{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T19:34:45Z","timestamp":1772825685188,"version":"3.50.1"},"reference-count":180,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Colloids and Surfaces B: Biointerfaces"],"published-print":{"date-parts":[[2022,1]]},"DOI":"10.1016\/j.colsurfb.2021.112157","type":"journal-article","created":{"date-parts":[[2021,10,13]],"date-time":"2021-10-13T15:01:25Z","timestamp":1634137285000},"page":"112157","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"special_numbering":"P1","title":["Amyloidogenicity of peptides targeting diabetes and obesity"],"prefix":"10.1016","volume":"209","author":[{"given":"Lu\u00eds Maur\u00edcio T.R.","family":"Lima","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luis Pe\u00f1a","family":"Icart","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"7","key":"10.1016\/j.colsurfb.2021.112157_bib1","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1007\/s11095-020-02817-9","article-title":"Influence of production process and scale on quality of polypeptide drugs: a case study on GLP-1 analogs","volume":"37","author":"Arne","year":"2020","journal-title":"Pharm. Res."},{"key":"10.1016\/j.colsurfb.2021.112157_bib2","doi-asserted-by":"crossref","first-page":"42669","DOI":"10.1074\/jbc.M504298200","article-title":"Early events in the fibrillation of monomeric insulin","volume":"280","author":"Ahmad","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib3","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1055\/s-2004-826178","article-title":"GLP-1 receptor agonists and DPP-4 inhibitors in the treatment of type 2 diabetes","volume":"36","author":"Ahr\u00e9n","year":"2004","journal-title":"Horm. Metab. Res. Horm. Stoffwechselforschung Horm. Metab."},{"key":"10.1016\/j.colsurfb.2021.112157_bib4","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.ijbiomac.2017.05.048","article-title":"Protein aggregation: from background to inhibition strategies","volume":"103","author":"Alam","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib5","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1016\/j.diabres.2006.07.013","article-title":"Severe insulin resistance associated with subcutaneous amyloid deposition","volume":"75","author":"Albert","year":"2007","journal-title":"Diabetes Res. Clin. Pract."},{"key":"10.1016\/j.colsurfb.2021.112157_bib6","doi-asserted-by":"crossref","first-page":"834","DOI":"10.15537\/smj.2016.8.15800","article-title":"A review of glycemic efficacy of liraglutide once daily in achieving glycated hemoglobin targets compared with exenatide twice daily, or sitagliptin once daily in the treatment of type 2 diabetes","volume":"37","author":"Alshali","year":"2016","journal-title":"Saudi Med. J."},{"key":"10.1016\/j.colsurfb.2021.112157_bib7","doi-asserted-by":"crossref","first-page":"S53","DOI":"10.2337\/dc21-S005","article-title":"5. Facilitating behavior change and well-being to improve health outcomes: standards of medical care in diabetes\u20142021","volume":"44","author":"American Diabetes Association","year":"2021","journal-title":"Diabetes Care"},{"key":"10.1016\/j.colsurfb.2021.112157_bib8","unstructured":"Amylin analogs [WWW Document], 2020. Zealand Pharma. URL https:\/\/www.zealandpharma.com\/publications-amylin. (Accessed 5 October 2021)."},{"key":"10.1016\/j.colsurfb.2021.112157_bib9","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1016\/j.jmb.2010.02.012","article-title":"Glucagon fibril polymorphism reflects differences in protofilament backbone structure","volume":"397","author":"Andersen","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib10","doi-asserted-by":"crossref","first-page":"7314","DOI":"10.1021\/bi6025374","article-title":"Glucagon amyloid-like fibril morphology is selected via morphology-dependent growth inhibition","volume":"46","author":"Andersen","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.colsurfb.2021.112157_bib11","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1111\/dom.14302","article-title":"ADO09, a co-formulation of the amylin analogue pramlintide and the insulin analogue A21G, lowers postprandial blood glucose versus insulin lispro in type 1 diabetes","volume":"23","author":"Andersen","year":"2021","journal-title":"Diabetes Obes. Metab."},{"key":"10.1016\/j.colsurfb.2021.112157_bib12","doi-asserted-by":"crossref","first-page":"183","DOI":"10.2337\/diaspect.17.3.183","article-title":"Glucose metabolism and regulation: beyond insulin and glucagon","volume":"17","author":"Aronoff","year":"2004","journal-title":"Diabetes Spectr."},{"key":"10.1016\/j.colsurfb.2021.112157_bib13","series-title":"A Comprehensive Guide to Toxicology in Nonclinical Drug Development","first-page":"109","article-title":"Chapter 5 - Acute, Subacute, Subchronic, and Chronic General Toxicity Testing for Preclinical Drug Development","author":"Denny","year":"2017"},{"issue":"2","key":"10.1016\/j.colsurfb.2021.112157_bib14","doi-asserted-by":"crossref","first-page":"e0245372","DOI":"10.1371\/journal.pone.0245372","article-title":"Heat-stability study of various insulin types in tropical temperature conditions: new insights towards improving diabetes care","volume":"16","author":"Kaufmann","year":"2021","journal-title":"PLOS One"},{"key":"10.1016\/j.colsurfb.2021.112157_bib15","doi-asserted-by":"crossref","first-page":"5271","DOI":"10.1021\/la400612w","article-title":"Vortex-induced amyloid superstructures of insulin and its component A and B chains","volume":"29","author":"Babenko","year":"2013","journal-title":"Langmuir"},{"key":"10.1016\/j.colsurfb.2021.112157_bib16","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.ab.2016.08.002","article-title":"Identifying protein aggregation mechanisms and quantifying aggregation rates from combined monomer depletion and continuous scattering","volume":"511","author":"Barnett","year":"2016","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib17","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.bpc.2015.07.002","article-title":"Aggregate structure, morphology and the effect of aggregation mechanisms on viscosity at elevated protein concentrations","volume":"207","author":"Barnett","year":"2015","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib18","first-page":"8","article-title":"New uses and formulations of glucagon for hypoglycaemia","author":"Beato-V\u00edbora","year":"2019","journal-title":"Drugs Context"},{"key":"10.1016\/j.colsurfb.2021.112157_bib19","doi-asserted-by":"crossref","first-page":"1687","DOI":"10.1016\/S0140-6736(21)00944-2","article-title":"Cagrilintide plus semaglutide for obesity management","volume":"397","author":"Becerril","year":"2021","journal-title":"Lancet"},{"key":"10.1016\/j.colsurfb.2021.112157_bib20","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1080\/13506129.2020.1835263","article-title":"Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee","volume":"27","author":"Benson","year":"2020","journal-title":"Amyloid"},{"key":"10.1016\/j.colsurfb.2021.112157_bib21","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bss0680001","article-title":"Protein folding and its links with human disease","volume":"68","author":"Berry","year":"2001","journal-title":"Biochem. Soc. Symp."},{"key":"10.1016\/j.colsurfb.2021.112157_bib22","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S2213-8587(17)30412-6","article-title":"Cardiovascular outcomes with glucagon-like peptide-1 receptor agonists in patients with type 2 diabetes: a meta-analysis","volume":"6","author":"Bethel","year":"2018","journal-title":"Lancet Diabetes Endocrinol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib23","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1016\/j.bbapap.2010.04.001","article-title":"Molecular mechanism of thioflavin-T binding to amyloid fibrils","volume":"1804","author":"Biancalana","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.colsurfb.2021.112157_bib24","doi-asserted-by":"crossref","DOI":"10.3171\/2016.5.FOCUS15126","article-title":"Human prion diseases: surgical lessons learned from iatrogenic prion transmission","volume":"41","author":"Bonda","year":"2016","journal-title":"Neurosurg. Focus"},{"key":"10.1016\/j.colsurfb.2021.112157_bib25","doi-asserted-by":"crossref","first-page":"2153","DOI":"10.1021\/acs.molpharmaceut.9b00106","article-title":"Peptide oligomerization memory effects and their impact on the physical stability of the GLP-1 agonist liraglutide","volume":"16","author":"Bothe","year":"2019","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.colsurfb.2021.112157_bib26","first-page":"1","article-title":"Molecular confinement of human amylin in lipidic nanoparticles","author":"Braga","year":"2015","journal-title":"J. Liposome Res."},{"key":"10.1016\/j.colsurfb.2021.112157_bib27","series-title":"Galenics of Insulin","author":"Brange","year":"1987"},{"key":"10.1016\/j.colsurfb.2021.112157_bib28","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/j.bpj.2010.09.070","article-title":"Biphasic effects of insulin on islet amyloid polypeptide membrane disruption","volume":"100","author":"Brender","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/j.colsurfb.2021.112157_bib29","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1021\/ar200189b","article-title":"Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective","volume":"45","author":"Brender","year":"2012","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.colsurfb.2021.112157_bib30","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1111\/ijcp.12361","article-title":"GLP-1 receptor agonists vs. DPP-4 inhibitors for type 2 diabetes: is one approach more successful or preferable than the other?","volume":"68","author":"Brunton","year":"2014","journal-title":"Int. J. Clin. Pract"},{"key":"10.1016\/j.colsurfb.2021.112157_bib31","doi-asserted-by":"crossref","first-page":"102","DOI":"10.2337\/diabetes.52.1.102","article-title":"\u03b2-cell deficit and increased \u03b2-cell apoptosis in humans with type 2 diabetes","volume":"52","author":"Butler","year":"2003","journal-title":"Diabetes"},{"key":"10.1016\/j.colsurfb.2021.112157_bib32","series-title":"Advances in Protein Chemistry and Structural Biology","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/bs.apcsb.2019.09.002","article-title":"Functional and dysfunctional folding, association and aggregation of caseins","author":"Carver","year":"2019"},{"key":"10.1016\/j.colsurfb.2021.112157_bib33","doi-asserted-by":"crossref","DOI":"10.1016\/j.bpc.2020.106505","article-title":"Visualizing and trapping transient oligomers in amyloid assembly pathways","volume":"268","author":"Cawood","year":"2021","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib34","doi-asserted-by":"crossref","first-page":"14588","DOI":"10.1021\/bi00044a038","article-title":"Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitro","volume":"34","author":"Charge","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.colsurfb.2021.112157_bib35","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.jim.2017.09.004","article-title":"Development and validation of a cell based assay for the detection of neutralizing antibodies against recombinant insulins","volume":"452","author":"Chatterjee","year":"2018","journal-title":"J. Immunol. Methods"},{"key":"10.1016\/j.colsurfb.2021.112157_bib36","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1111\/j.1464-5491.1991.tb01675.x","article-title":"Autoantibodies to islet amyloid polypeptide in diabetes","volume":"8","author":"Clark","year":"1991","journal-title":"Diabet. Med. J. Br. Diabet. Assoc."},{"key":"10.1016\/j.colsurfb.2021.112157_bib37","doi-asserted-by":"crossref","first-page":"1202","DOI":"10.1038\/1831202a0","article-title":"Electron microscopic observations on a fibrous component in amyloid of diverse origins","volume":"183","author":"Cohen","year":"1959","journal-title":"Nature"},{"key":"10.1016\/j.colsurfb.2021.112157_bib38","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/0306-9877(91)90150-W","article-title":"Amylin and insulin co-replacement therapy for insulin-dependent (type I) diabetes mellitus","volume":"36","author":"Cooper","year":"1991","journal-title":"Med. Hypotheses"},{"key":"10.1016\/j.colsurfb.2021.112157_bib39","doi-asserted-by":"crossref","first-page":"8628","DOI":"10.1073\/pnas.84.23.8628","article-title":"Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients","volume":"84","author":"Cooper","year":"1987","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.colsurfb.2021.112157_bib40","doi-asserted-by":"crossref","unstructured":"Cooper, G.J.S., Willis, A.C., Amylin Pharmaceuticals, I., 1989. Amylin peptides.","DOI":"10.1038\/340272b0"},{"key":"10.1016\/j.colsurfb.2021.112157_bib41","unstructured":"Cooper, T., Ainsberg, A., 2011. Breakthrough: Elizabeth Hughes, the Discovery of Insulin, and the Making of a Medical Miracle, Reprint edition. ed. St. Martin\u2019s Griffin, New York."},{"issue":"3","key":"10.1016\/j.colsurfb.2021.112157_bib42","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1021\/acs.chemrev.0c00981","article-title":"Proteostasis of islet amyloid polypeptide: a molecular perspective of risk factors and protective strategies for type II diabetes","volume":"121","author":"Milardi","year":"2021","journal-title":"Chem. Rev."},{"key":"10.1016\/j.colsurfb.2021.112157_bib43","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bpc.2016.09.007","article-title":"Amyloidogenesis of the amylin analogue pramlintide","volume":"219","author":"da Silva","year":"2016","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib44","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bpc.2016.09.007","article-title":"Amyloidogenesis of the amylin analogue pramlintide","volume":"219","author":"da Silva","year":"2016","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib45","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1016\/j.ijpharm.2018.06.039","article-title":"Physico-chemical properties of co-formulated fast-acting insulin with pramlintide","volume":"547","author":"da Silva","year":"2018","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.colsurfb.2021.112157_bib46","article-title":"Human amylin analogues","volume":"WO2013156594A1.","author":"Dahl","year":"2013","journal-title":"Patent"},{"key":"10.1016\/j.colsurfb.2021.112157_bib47","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.2337\/diabetes.53.9.2181","article-title":"Therapeutic strategies based on glucagon-like peptide 1","volume":"53","author":"Deacon","year":"2004","journal-title":"Diabetes"},{"key":"10.1016\/j.colsurfb.2021.112157_bib48","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1007\/s001250050903","article-title":"Dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity","volume":"41","author":"Deacon","year":"1998","journal-title":"Diabetologia"},{"key":"10.1016\/j.colsurfb.2021.112157_bib49","unstructured":"Demmer, O., Just, R., Giehm, L., Skarbaliene, J., Mathiesen, J.M., 2015. Amylin analogues. WO2015040182A2."},{"key":"10.1016\/j.colsurfb.2021.112157_bib50","doi-asserted-by":"crossref","first-page":"R57","DOI":"10.1530\/JME-17-0138","article-title":"IAPP and type 1 diabetes: implications for immunity, metabolism and islet transplants","volume":"60","author":"Denroche","year":"2018","journal-title":"J. Mol. Endocrinol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib51","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1007\/BF00276849","article-title":"Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient","volume":"31","author":"Dische","year":"1988","journal-title":"Diabetologia"},{"key":"10.1016\/j.colsurfb.2021.112157_bib52","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/nature02261","article-title":"Protein folding and misfolding","volume":"426","author":"Dobson","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.colsurfb.2021.112157_bib53","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0968-0004(99)01445-0","article-title":"Protein misfolding, evolution and disease","volume":"24","author":"Dobson","year":"1999","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.colsurfb.2021.112157_bib54","first-page":"71","article-title":"Pharmaceutical amyloidosis associated with subcutaneous insulin and enfuvirtide administration","volume":"21","author":"D\u2019Souza","year":"2014","journal-title":"Amyloid Int. J. Exp. Clin. Investig. Off. J. Int. Soc. Amyloidosis"},{"key":"10.1016\/j.colsurfb.2021.112157_bib55","doi-asserted-by":"crossref","unstructured":"Effects of Intensive Glucose Lowering in Type 2 Diabetes, 2008. N. Engl. J. Med. 358, 2545\u20132559. https:\/\/doi.org\/10.1056\/NEJMoa0802743.","DOI":"10.1056\/NEJMoa0802743"},{"key":"10.1016\/j.colsurfb.2021.112157_bib56","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijpharm.2019.118923","article-title":"Inhibiting the fibrillation of a GLP-1-like peptide","volume":"574","author":"Egbu","year":"2020","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.colsurfb.2021.112157_bib57","doi-asserted-by":"crossref","first-page":"0","DOI":"10.1016\/S0140-6736(21)00845-X","article-title":"Safety, tolerability, pharmacokinetics, and pharmacodynamics of concomitant administration of multiple doses of cagrilintide with semaglutide 2\u00b74 mg for weight management: a randomised, controlled, phase 1b trial","volume":"397","author":"Enebo","year":"2021","journal-title":"Lancet"},{"key":"10.1016\/j.colsurfb.2021.112157_bib58","doi-asserted-by":"crossref","first-page":"7402","DOI":"10.1016\/S0021-9258(18)42531-8","article-title":"Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas","volume":"267","author":"Eng","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib59","unstructured":"Engelund, D.K., Jensen, S.S., Lundqvist, J., 2020. Stable semaglutide compositions and uses thereof. WO2020084126A1."},{"key":"10.1016\/j.colsurfb.2021.112157_bib60","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.bpc.2016.09.008","article-title":"Regulation of the assembly and amyloid aggregation of murine amylin by zinc","volume":"218","author":"Erthal","year":"2016","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib61","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.bpc.2016.09.008","article-title":"Regulation of the assembly and amyloid aggregation of murine amylin by zinc","volume":"218","author":"Erthal","year":"2016","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib62","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1210\/jcem-19-9-1055","article-title":"Resistance to insulin due to neutralizing antibodies","volume":"19","author":"Ezrin","year":"1959","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.colsurfb.2021.112157_bib63","doi-asserted-by":"crossref","first-page":"5682","DOI":"10.1093\/emboj\/cdf573","article-title":"The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation","volume":"21","author":"F\u00e4ndrich","year":"2002","journal-title":"EMBO J"},{"key":"10.1016\/j.colsurfb.2021.112157_bib64","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1038\/35065514","article-title":"Amyloid fibrils from muscle myoglobin","volume":"410","author":"F\u00e4ndrich","year":"2001","journal-title":"Nature"},{"key":"10.1016\/j.colsurfb.2021.112157_bib65","series-title":"Bittersweet: Diabetes, Insulin, and the Transformation of Illness","author":"Feudtner","year":"2003"},{"key":"10.1016\/j.colsurfb.2021.112157_bib66","series-title":"Meyler\u2019s Side Effects of Endocrine and Metabolic Drugs","author":"Aronson","year":"2009"},{"key":"10.1016\/j.colsurfb.2021.112157_bib67","doi-asserted-by":"crossref","first-page":"1202","DOI":"10.1016\/j.bpj.2015.07.051","article-title":"Oligomerization of a glucagon-like peptide 1 analog: bridging experiment and simulations","volume":"109","author":"Frederiksen","year":"2015","journal-title":"Biophys. J."},{"key":"10.1016\/j.colsurfb.2021.112157_bib68","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1097\/NHH.0000000000000446","article-title":"A review of insulin for the treatment of diabetes mellitus","volume":"34","author":"Freeland","year":"2016","journal-title":"Home Healthc. Now"},{"key":"10.1016\/j.colsurfb.2021.112157_bib69","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1038\/nrd1695","article-title":"Protein drug stability: a formulation challenge","volume":"4","author":"Frokjaer","year":"2005","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.colsurfb.2021.112157_bib70","unstructured":"Gaeta, L.S.L., Jones, H., Albrecht, E., Corporation, A., 1997. Pramlintide pro H-amylin salts and compositions."},{"key":"10.1016\/j.colsurfb.2021.112157_bib71","doi-asserted-by":"crossref","first-page":"8338","DOI":"10.1039\/C4CP04682J","article-title":"Modulation of human IAPP fibrillation: cosolutes, crowders and chaperones","volume":"17","author":"Gao","year":"2015","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.colsurfb.2021.112157_bib72","doi-asserted-by":"crossref","first-page":"1080","DOI":"10.1007\/BF02221685","article-title":"Detection of autoantibodies against islet amyloid polypeptide in human serum. Lack of association with type 1 (insulin-dependent) diabetes mellitus, or with conditions favouring amyloid deposition in islets. The Belgian Diabetes Registry","volume":"35","author":"Gorus","year":"1992","journal-title":"Diabetologia"},{"key":"10.1016\/j.colsurfb.2021.112157_bib73","first-page":"2017","article-title":"Localized subcutaneous insulin-derived amyloidosis excised after evaluation using ultrasonography in a patient with type 2 diabetes mellitus","author":"Hagiwara","year":"2017","journal-title":"Case Rep. Endocrinol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib74","doi-asserted-by":"crossref","first-page":"210","DOI":"10.2337\/db18-210-OR","article-title":"Insulin-plus-pramlintide artificial pancreas in type 1 diabetes\u2014randomized controlled trial","volume":"67","author":"Haidar","year":"2018","journal-title":"Diabetes"},{"key":"10.1016\/j.colsurfb.2021.112157_bib75","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1007\/s13300-018-0373-9","article-title":"Effectiveness and safety of a novel care model for the management of type 2 diabetes at 1 year: an open-label, non-randomized, controlled study","volume":"9","author":"Hallberg","year":"2018","journal-title":"Diabetes Ther."},{"key":"10.1016\/j.colsurfb.2021.112157_bib76","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/S2468-1253(16)30106-6","article-title":"Type 3c (pancreatogenic) diabetes mellitus secondary to chronic pancreatitis and pancreatic cancer","volume":"1","author":"Hart","year":"2016","journal-title":"Lancet Gastroenterol. Hepatol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib77","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1124\/pr.115.010629","article-title":"Amylin: pharmacology, physiology, and clinical potential","volume":"67","author":"Hay","year":"2015","journal-title":"Pharmacol. Rev."},{"key":"10.1016\/j.colsurfb.2021.112157_bib78","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1210\/endrev\/bnaa015","article-title":"The evolution of insulin and how it informs therapy and treatment choices","volume":"41","author":"Hirsch","year":"2020","journal-title":"Endocr. Rev"},{"key":"10.1016\/j.colsurfb.2021.112157_bib79","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.sbi.2017.03.002","article-title":"Ion mobility-mass spectrometry and orthogonal gas-phase techniques to study amyloid formation and inhibition","volume":"46","author":"Hoffmann","year":"2017","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib80","doi-asserted-by":"crossref","first-page":"1409","DOI":"10.1152\/physrev.00034.2006","article-title":"The physiology of glucagon-like peptide 1","volume":"87","author":"Holst","year":"2007","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.colsurfb.2021.112157_bib81","doi-asserted-by":"crossref","first-page":"1409","DOI":"10.1152\/physrev.00034.2006","article-title":"The physiology of glucagon-like peptide 1","volume":"87","author":"Holst","year":"2007","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.colsurfb.2021.112157_bib82","first-page":"5","article-title":"In search of aggregation pathways of IAPP and other amyloidogenic proteins: finding answers through NMR spectroscopy","author":"Hr","year":"2014","journal-title":"J. Phys. Chem. Lett."},{"key":"10.1016\/j.colsurfb.2021.112157_bib83","first-page":"8","article-title":"Applications of mass spectrometry in the onset of amyloid fibril formation: focus on the analysis of early-stage oligomers","author":"Hu","year":"2020","journal-title":"Front. Chem"},{"key":"10.1016\/j.colsurfb.2021.112157_bib84","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1002\/bip.20126","article-title":"Exenatide: NMR\/CD evaluation of the medium dependence of conformation and aggregation state","volume":"76","author":"Hudson","year":"2004","journal-title":"Pept. Sci."},{"key":"10.1016\/j.colsurfb.2021.112157_bib85","doi-asserted-by":"crossref","unstructured":"Idris, I., n.d. Novel development of a co-formulation of insulin and Amylin. Diabetes Obes. Metab. Now n\/a. https:\/\/doi.org\/10.1002\/doi2.00015.","DOI":"10.1002\/doi2.00015"},{"key":"10.1016\/j.colsurfb.2021.112157_bib86","doi-asserted-by":"crossref","DOI":"10.1016\/j.bpc.2020.106507","article-title":"Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology","volume":"269","author":"Ivanova","year":"2021","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib87","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1186\/s12902-019-0385-0","article-title":"Toxicity of insulin-derived amyloidosis: a case report","volume":"19","author":"Iwaya","year":"2019","journal-title":"BMC Endocr. Disord."},{"key":"10.1016\/j.colsurfb.2021.112157_bib88","first-page":"25","article-title":"Amyloidosis produced by injections of proteins","volume":"1","author":"Jaff\u00e9","year":"1926","journal-title":"Arch. Pathol. Lab. Med."},{"key":"10.1016\/j.colsurfb.2021.112157_bib89","doi-asserted-by":"crossref","first-page":"491","DOI":"10.2337\/diabetes.48.3.491","article-title":"The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles","volume":"48","author":"Janson","year":"1999","journal-title":"Diabetes"},{"key":"10.1016\/j.colsurfb.2021.112157_bib90","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1038\/nature15369","article-title":"Evidence for human transmission of amyloid-\u03b2 pathology and cerebral amyloid angiopathy","volume":"525","author":"Jaunmuktane","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.colsurfb.2021.112157_bib91","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1016\/j.bbamem.2007.01.022","article-title":"Membrane interaction of islet amyloid polypeptide","volume":"1768","author":"Jayasinghe","year":"2007","journal-title":"Biochim. Biophys. Acta BBA - Biomembr.\u00a0Amyloidogenic Protein\u2013Membrane Interaction"},{"key":"10.1016\/j.colsurfb.2021.112157_bib92","doi-asserted-by":"crossref","DOI":"10.1016\/j.domaniend.2020.106532","article-title":"Amyloidogenesis of feline amylin and plasma levels in cats with diabetes mellitus or pancreatitis","volume":"74","author":"Jotha-Mattos","year":"2021","journal-title":"Domest. Anim. Endocrinol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib93","doi-asserted-by":"crossref","first-page":"1803","DOI":"10.1016\/j.bbamem.2018.01.015","article-title":"Serum albumin impedes the amyloid aggregation and hemolysis of human islet amyloid polypeptide and alpha synuclein","volume":"1860","author":"Kakinen","year":"2018","journal-title":"Biochim. Biophys. Acta BBA - Biomembr.\u00a0Protein Aggregation and Misfolding at the Cell Membrane Interface"},{"key":"10.1016\/j.colsurfb.2021.112157_bib94","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/s13340-018-0347-1","article-title":"IAPP\/amylin and \u03b2-cell failure: implication of the risk factors of type 2 diabetes","volume":"9","author":"Kanatsuka","year":"2018","journal-title":"Diabetol. Int."},{"key":"10.1016\/j.colsurfb.2021.112157_bib95","doi-asserted-by":"crossref","DOI":"10.1016\/j.chemphyslip.2021.105083","article-title":"Investigation of the effects of two major secretory granules components, insulin and zinc, on human-IAPP amyloid aggregation and membrane damage","volume":"237","author":"Khemtemourian","year":"2021","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.colsurfb.2021.112157_bib96","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1111\/jdi.12607","article-title":"Lessons from a cardiovascular outcome trial with liraglutide in type 2 diabetes","volume":"8","author":"Kim","year":"2017","journal-title":"J. Diabetes Investig."},{"key":"10.1016\/j.colsurfb.2021.112157_bib97","first-page":"7","article-title":"Role and cytotoxicity of amylin and protection of pancreatic islet \u03b2-cells from amylin cytotoxicity","author":"Kiriyama","year":"2018","journal-title":"Cells"},{"key":"10.1016\/j.colsurfb.2021.112157_bib98","doi-asserted-by":"crossref","first-page":"155","DOI":"10.3389\/fendo.2019.00155","article-title":"The discovery and development of liraglutide and semaglutide","volume":"10","author":"Knudsen","year":"2019","journal-title":"Front. Endocrinol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib99","unstructured":"Lau, D., McFarlane, J., Erichsen, I., Fransisco, A.M., Le Roux, C., McGowan, B., Pedersen, S., Pietil\u00e4inen, K., Rubino, D.M., Satylganova, A., n.d. Efficacy and Safety of AM833 for Weight Loss: A Dose-finding Trial in Adults With Overweight\/Obesity [WWW Document]. URL \u3008https:\/\/tos.planion.com\/Web.User\/AbstractDet?ACCOUNT=TOS&ABSID=23842&CONF=OW2020&ssoOverride=OFF&CKEY\u3009 (Accessed 5 October 2021)."},{"key":"10.1016\/j.colsurfb.2021.112157_bib100","doi-asserted-by":"crossref","first-page":"7370","DOI":"10.1021\/acs.jmedchem.5b00726","article-title":"Discovery of the once-weekly glucagon-like peptide-1 (GLP-1) analogue semaglutide","volume":"58","author":"Lau","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib101","doi-asserted-by":"crossref","DOI":"10.1542\/peds.2017-3349","article-title":"Management of type 1 diabetes with a very low\u2013carbohydrate diet","volume":"141","author":"Lennerz","year":"2018","journal-title":"Pediatrics"},{"key":"10.1016\/j.colsurfb.2021.112157_bib102","doi-asserted-by":"crossref","first-page":"8447","DOI":"10.1038\/s41598-019-44591-8","article-title":"Combined Amylin\/GLP-1 pharmacotherapy to promote and sustain long-lasting weight loss","volume":"9","author":"Liberini","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.colsurfb.2021.112157_bib103","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.tem.2018.01.011","article-title":"Glucagon-like peptide-1 receptor agonists and cardiovascular events: class effects versus individual patterns","volume":"29","author":"Lim","year":"2018","journal-title":"Trends Endocrinol. Metab."},{"key":"10.1016\/j.colsurfb.2021.112157_bib104","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1001\/jama.2017.6939","article-title":"Human insulin for type 2 diabetes: an effective, less-expensive option","volume":"318","author":"Lipska","year":"2017","journal-title":"JAMA"},{"key":"10.1016\/j.colsurfb.2021.112157_bib105","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1039\/C1CC14285B","article-title":"Co-assembly of human islet amyloid polypeptide (hIAPP)\/insulin","volume":"48","author":"Liu","year":"2012","journal-title":"Chem. Commun. Camb. Engl."},{"key":"10.1016\/j.colsurfb.2021.112157_bib106","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1039\/C1CC14285B","article-title":"Co-assembly of human islet amyloid polypeptide (hIAPP)\/insulin","volume":"48","author":"Liu","year":"2011","journal-title":"Chem. Commun."},{"key":"10.1016\/j.colsurfb.2021.112157_bib107","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.jinorgbio.2017.06.008","article-title":"Zn(II) \u2013 pramlintide: stability, binding sites and unexpected aggregation","volume":"174","author":"\u0141oboda","year":"2017","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib108","doi-asserted-by":"crossref","first-page":"3132","DOI":"10.1529\/biophysj.107.110635","article-title":"Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy","volume":"93","author":"Lopes","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.colsurfb.2021.112157_bib109","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1038\/368756a0","article-title":"Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus","volume":"368","author":"Lorenzo","year":"1994","journal-title":"Nature"},{"key":"10.1016\/j.colsurfb.2021.112157_bib110","unstructured":"Ludvigsen, S., Schlein, M., B\u00f8ving, T.E.G., Bonde, C., Lille\u00f8re, A.-M., Engelund, D.K., Nielsen, B.R., 2014. Stable formulations of peptides. US8748376B2."},{"key":"10.1016\/j.colsurfb.2021.112157_bib111","unstructured":"Ludvigsen, S., Schlein, M., B\u00d8VING, T.E.G., Bonde, C., LILLE\u00d8RE, A.-M., Engelund, D.K., NIELSEN, B.R., 2006. Stable formulations of insulinoptropic peptides. WO2006051110A2."},{"key":"10.1016\/j.colsurfb.2021.112157_bib112","doi-asserted-by":"crossref","first-page":"2880","DOI":"10.1038\/srep02880","article-title":"Mechanism of amyloid \u03b2\u2212protein dimerization determined using single\u2212molecule AFM force spectroscopy","volume":"3","author":"Lv","year":"2013","journal-title":"Sci. Rep."},{"key":"10.1016\/j.colsurfb.2021.112157_bib113","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1038\/ijo.2009.238","article-title":"Davalintide (AC2307), a novel amylin-mimetic peptide: enhanced pharmacological properties over native amylin to reduce food intake and body weight","volume":"34","author":"Mack","year":"2010","journal-title":"Int. J. Obes."},{"key":"10.1016\/j.colsurfb.2021.112157_bib114","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/s11095-018-2494-2","article-title":"The use of surfactants to solubilise a glucagon analogue","volume":"35","author":"Madsen","year":"2018","journal-title":"Pharm. Res."},{"key":"10.1016\/j.colsurfb.2021.112157_bib115","doi-asserted-by":"crossref","first-page":"2909","DOI":"10.1002\/jps.21566","article-title":"Protein aggregation: pathways, induction factors and analysis","volume":"98","author":"Mahler","year":"2009","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.colsurfb.2021.112157_bib116","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/s41551-020-0555-4","article-title":"A co-formulation of supramolecularly stabilized insulin and pramlintide enhances mealtime glucagon suppression in diabetic pigs","volume":"4","author":"Maikawa","year":"2020","journal-title":"Nat. Biomed. Eng."},{"key":"10.1016\/j.colsurfb.2021.112157_bib117","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.ijpharm.2011.04.024","article-title":"Probing the mechanism of insulin aggregation during agitation","volume":"413","author":"Malik","year":"2011","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.colsurfb.2021.112157_bib118","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1016\/j.talanta.2015.11.012","article-title":"New insights into side effect of solvents on the aggregation of human islet amyloid polypeptide 11\u201320","volume":"148","author":"Mao","year":"2016","journal-title":"Talanta"},{"key":"10.1016\/j.colsurfb.2021.112157_bib119","doi-asserted-by":"crossref","first-page":"8478","DOI":"10.1021\/bi300574r","article-title":"Ionic strength effects on amyloid formation by amylin are a complicated interplay among debye screening, ion selectivity, and hofmeister effects","volume":"51","author":"Marek","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.colsurfb.2021.112157_bib120","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1056\/NEJMoa1603827","article-title":"Liraglutide and cardiovascular outcomes in type 2 diabetes","volume":"375","author":"Marso","year":"2016","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.colsurfb.2021.112157_bib121","first-page":"11","article-title":"Amylin and calcitonin: potential therapeutic strategies to reduce body weight and liver fat","author":"Mathiesen","year":"2021","journal-title":"Front. Endocrinol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib122","unstructured":"Mathiesen, J.M., Villadsen, J.S., Giehm, L., Munch, H.K., Hamprecht, D.W., Heim-Riether, A., Fossati, G., 2018. Amylin analogues. US10071140B2."},{"key":"10.1016\/j.colsurfb.2021.112157_bib123","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1038\/mp.2016.230","article-title":"Molecular interaction between type 2 diabetes and Alzheimer\u2019s disease through cross-seeding of protein misfolding","volume":"22","author":"Moreno-Gonzalez","year":"2017","journal-title":"Mol. Psychiatry."},{"key":"10.1016\/j.colsurfb.2021.112157_bib124","doi-asserted-by":"crossref","first-page":"515","DOI":"10.7326\/0003-4819-151-7-200910060-00017","article-title":"Localized amyloidosis at the site of enfuvirtide injection","volume":"151","author":"Morilla","year":"2009","journal-title":"Ann. Intern. Med."},{"key":"10.1016\/j.colsurfb.2021.112157_bib125","doi-asserted-by":"crossref","first-page":"360","DOI":"10.3399\/bjgp19X704525","article-title":"Adapting diabetes medication for low carbohydrate management of type 2 diabetes: a practical guide","volume":"69","author":"Murdoch","year":"2019","journal-title":"Br. J. Gen. Pract."},{"key":"10.1016\/j.colsurfb.2021.112157_bib126","first-page":"253","article-title":"The quaternary structure of insulin glargine and glulisine under formulation conditions","author":"Nagel","year":"2019","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib127","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.amjmed.2013.10.029","article-title":"Insulin-derived amyloidosis and poor glycemic control: a case series","volume":"127","author":"Nagase","year":"2014","journal-title":"Am. J. Med."},{"key":"10.1016\/j.colsurfb.2021.112157_bib128","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1016\/S0006-3495(00)76359-4","article-title":"Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry","volume":"79","author":"Nettleton","year":"2000","journal-title":"Biophys. J."},{"key":"10.1016\/j.colsurfb.2021.112157_bib129","unstructured":"New USP Chapters regarding Testing for Subvisible Particles - ECA Academy [WWW Document], n.d. URL \u3008https:\/\/www.gmp-compliance.org\/gmp-news\/new-usp-chapters-regarding-testing-for-subvisible-particles\u3009 (Accessed 30 March\u00a02021)."},{"key":"10.1016\/j.colsurfb.2021.112157_bib130","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1021\/acs.chemrev.0c01122","article-title":"Amyloid oligomers: a joint experimental\/computational perspective on Alzheimer\u2019s Disease, Parkinson\u2019s Disease, Type II diabetes, and amyotrophic lateral sclerosis","volume":"121","author":"Nguyen","year":"2021","journal-title":"Chem. Rev"},{"key":"10.1016\/j.colsurfb.2021.112157_bib131","doi-asserted-by":"crossref","first-page":"6036","DOI":"10.1021\/bi002555c","article-title":"Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism","volume":"40","author":"Nielsen","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.colsurfb.2021.112157_bib132","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1080\/13506129.2016.1179183","article-title":"Insulin amyloid at injection sites of patients with diabetes","volume":"23","author":"Nilsson","year":"2016","journal-title":"Amyloid"},{"key":"10.1016\/j.colsurfb.2021.112157_bib133","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.chroma.2005.11.130","article-title":"Structural transition of glucagon in the concentrated solution observed by electrophoretic and spectroscopic techniques","volume":"1109","author":"Onoue","year":"2006","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.colsurfb.2021.112157_bib134","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1023\/B:PHAM.0000033016.36825.2c","article-title":"Mishandling of the therapeutic peptide glucagon generates cytotoxic amyloidogenic fibrils","volume":"21","author":"Onoue","year":"2004","journal-title":"Pharm. Res."},{"issue":"34","key":"10.1016\/j.colsurfb.2021.112157_bib135","first-page":"143","article-title":"WHO Drug Information 2020, vol. 34, 2 [full issue]","author":"Organization","year":"2020","journal-title":"WHO Drug Inf."},{"key":"10.1016\/j.colsurfb.2021.112157_bib136","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1177\/193229681000400609","article-title":"The nature of amyloid-like glucagon fibrils","volume":"4","author":"Pedersen","year":"2010","journal-title":"J. Diabetes Sci. Technol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib137","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/S0014-5793(01)02384-5","article-title":"Amyloid fibril formation by a helical cytochrome","volume":"495","author":"Pertinhez","year":"2001","journal-title":"FEBS Lett"},{"key":"10.1016\/j.colsurfb.2021.112157_bib138","doi-asserted-by":"crossref","first-page":"38","DOI":"10.5858\/2001-125-0038-TCCOA","article-title":"The changing concepts of amyloid","volume":"125","author":"Picken","year":"2001","journal-title":"Arch. Pathol. Lab. Med."},{"key":"10.1016\/j.colsurfb.2021.112157_bib139","doi-asserted-by":"crossref","first-page":"2455","DOI":"10.1038\/s41598-017-02597-0","article-title":"Effects of protein corona on IAPP amyloid aggregation, fibril remodelling, and cytotoxicity","volume":"7","author":"Pilkington","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.colsurfb.2021.112157_bib140","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2016\/2046327","article-title":"Inhibition of IAPP aggregation and toxicity by natural products and derivatives","volume":"2016","author":"Pithadia","year":"2016","journal-title":"J. Diabetes Res."},{"key":"10.1016\/j.colsurfb.2021.112157_bib141","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.2174\/092986609789839232","article-title":"Amyloidogenicity and aggregate cytotoxicity of human glucagon-like peptide-1 (hGLP-1)","volume":"16","author":"Poon","year":"2009","journal-title":"Protein Pept. Lett."},{"key":"10.1016\/j.colsurfb.2021.112157_bib142","doi-asserted-by":"crossref","first-page":"1500","DOI":"10.1016\/j.clinthera.2005.10.009","article-title":"Pramlintide in the treatment of type 1 and type 2 diabetes mellitus","volume":"27","author":"Ryan","year":"2005","journal-title":"Clin. Ther."},{"key":"10.1016\/j.colsurfb.2021.112157_bib143","unstructured":"Sch\u00e4ffer, L., Kruse, T., Lau, J., Th\u00f8gersen, H., 2010. Amylin derivatives. WO2010046357A1."},{"key":"10.1016\/j.colsurfb.2021.112157_bib144","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/j.bpj.2016.05.050","article-title":"The role of cholesterol in driving IAPP-membrane interactions","volume":"111","author":"Sciacca","year":"2016","journal-title":"Biophys. J."},{"key":"10.1016\/j.colsurfb.2021.112157_bib145","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1038\/nchem.2615","article-title":"An infrared spectroscopy approach to follow \u03b2-sheet formation in peptide amyloid assemblies","volume":"9","author":"Seo","year":"2017","journal-title":"Nat. Chem."},{"key":"10.1016\/j.colsurfb.2021.112157_bib146","first-page":"397","article-title":"Localized amyloidosis at the site of repeated insulin injection in a diabetic patient. Intern","volume":"49","author":"Shikama","year":"2010","journal-title":"Med. Tokyo Jpn."},{"key":"10.1016\/j.colsurfb.2021.112157_bib147","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1038\/206737a0","article-title":"Structure of amyloid fibrils after negative staining and high-resolution electron microscopy","volume":"206","author":"Shirahama","year":"1965","journal-title":"Nature"},{"key":"10.1016\/j.colsurfb.2021.112157_bib148","first-page":"8","article-title":"Key information related to quality by design (QbD) applications in analytical methods development","author":"Silva Ara\u00fajo","year":"2020","journal-title":"Braz. J. Anal. Chem"},{"key":"10.1016\/j.colsurfb.2021.112157_bib149","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1080\/10837450.2019.1621896","article-title":"Physico-chemical stability of co-formulation of PEGylated human amylin with insulin","volume":"24","author":"Sin\u00e9sia","year":"2019","journal-title":"Pharm. Dev. Technol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib150","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1007\/s10930-019-09877-w","article-title":"Heterotropic modulation of amylin fibrillation by small molecules: implications for formulative designs","volume":"39","author":"Sin\u00e9zia","year":"2020","journal-title":"Protein J."},{"key":"10.1016\/j.colsurfb.2021.112157_bib151","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0138803","article-title":"Monoconjugation of human amylin with methylpolyethyleneglycol","volume":"10","author":"Sisnande","year":"2015","journal-title":"PLOS One"},{"key":"10.1016\/j.colsurfb.2021.112157_bib152","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1002\/bit.260400805","article-title":"Mechanism of insulin aggregation and stabilization in agitated aqueous solutions","volume":"40","author":"Sluzky","year":"1992","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.colsurfb.2021.112157_bib153","doi-asserted-by":"crossref","first-page":"9377","DOI":"10.1073\/pnas.88.21.9377","article-title":"Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces","volume":"88","author":"Sluzky","year":"1991","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.colsurfb.2021.112157_bib154","doi-asserted-by":"crossref","first-page":"9377","DOI":"10.1073\/pnas.88.21.9377","article-title":"Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces","volume":"88","author":"Sluzky","year":"1991","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.colsurfb.2021.112157_bib155","doi-asserted-by":"crossref","first-page":"7079","DOI":"10.1021\/ja900285z","article-title":"Association of highly compact type II diabetes related islet amyloid polypeptide intermediate species at physiological temperature revealed by diffusion NMR spectroscopy","volume":"131","author":"Soong","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.colsurfb.2021.112157_bib156","doi-asserted-by":"crossref","first-page":"6304","DOI":"10.1021\/jacs.5b01673","article-title":"X-ray crystallographic structures of oligomers of peptides derived from \u03b22-microglobulin","volume":"137","author":"Spencer","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.colsurfb.2021.112157_bib157","first-page":"108","article-title":"Iatrogenic, insulin-dependent, local amyloidosis","volume":"48","author":"St\u00f6rkel","year":"1983","journal-title":"Lab. Investig. J. Tech. Methods Pathol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib158","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1016\/j.bpj.2019.12.028","article-title":"Primary and secondary binding of exenatide to liposomes","volume":"118","author":"Stulz","year":"2020","journal-title":"Biophys. J."},{"key":"10.1016\/j.colsurfb.2021.112157_bib159","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1007\/s00256-017-2749-8","article-title":"Imaging characteristics of subcutaneous amyloid deposits in diabetic patients: the \u201cinsulin ball","volume":"47","author":"Tanio","year":"2018","journal-title":"Skeletal Radiol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib160","doi-asserted-by":"crossref","first-page":"6704","DOI":"10.1021\/acs.biochem.5b00567","article-title":"Analysis of the ability of pramlintide to inhibit amyloid formation by human islet amyloid polypeptide reveals a balance between optimal recognition and reduced amyloidogenicity","volume":"54","author":"Wang","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.colsurfb.2021.112157_bib161","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.ijpharm.2010.02.025","article-title":"Protein aggregation\u2014pathways and influencing factors","volume":"390","author":"Wang","year":"2010","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.colsurfb.2021.112157_bib162","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1021\/mp500519s","article-title":"Transformation of oligomers of lipidated peptide induced by change in pH","volume":"12","author":"Wang","year":"2015","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.colsurfb.2021.112157_bib163","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1246\/bcsj.20150058","article-title":"Acceleration of insulin amyloid fibrillation at liquid\u2013liquid interfaces","volume":"88","author":"Watanabe","year":"2015","journal-title":"Bull. Chem. Soc. Jpn"},{"key":"10.1016\/j.colsurfb.2021.112157_bib164","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1021\/ja01206a030","article-title":"A fibrous modification of insulin. I. The heat precipitate of insulin","volume":"68","author":"Waugh","year":"1946","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.colsurfb.2021.112157_bib165","doi-asserted-by":"crossref","first-page":"2592","DOI":"10.1021\/ja01107a013","article-title":"Studies of the nucleation and growth reactions of selected types of insulin fibrils","volume":"75","author":"Waugh","year":"1953","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.colsurfb.2021.112157_bib166","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.toxrep.2014.11.019","article-title":"Phenolic excipients of insulin formulations induce cell death, pro-inflammatory signaling and MCP-1 release","volume":"2","author":"Weber","year":"2015","journal-title":"Toxicol. Rep."},{"key":"10.1016\/j.colsurfb.2021.112157_bib167","doi-asserted-by":"crossref","first-page":"5036","DOI":"10.1073\/pnas.87.13.5036","article-title":"Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation","volume":"87","author":"Westermark","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.colsurfb.2021.112157_bib168","doi-asserted-by":"crossref","first-page":"3881","DOI":"10.1073\/pnas.84.11.3881","article-title":"Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells","volume":"84","author":"Westermark","year":"1987","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.colsurfb.2021.112157_bib169","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1007\/BF00251821","article-title":"Islet amyloid in type 2 (non-insulin-dependent) diabetes is related to insulin","volume":"24","author":"Westermark","year":"1983","journal-title":"Diabetologia"},{"key":"10.1016\/j.colsurfb.2021.112157_bib170","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1093\/ajhp\/62.8.816","article-title":"Properties of pramlintide and insulin upon mixing","volume":"62","author":"Weyer","year":"2005","journal-title":"Am. J. Health. Syst. Pharm"},{"key":"10.1016\/j.colsurfb.2021.112157_bib171","unstructured":"Weyer, C., Laugero, K.D., Mack, C.M., Parkers, D.G., 2010. Compositions and methods for the control, prevention, and treatment of obesity and eating disorders. EP2248527A2."},{"key":"10.1016\/j.colsurfb.2021.112157_bib172","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1177\/1932296818757795","article-title":"Stable liquid glucagon: beyond emergency hypoglycemia rescue","volume":"12","author":"Wilson","year":"2018","journal-title":"J. Diabetes Sci. Technol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib173","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1016\/S0047-6374(02)00098-2","article-title":"Amyloid fibril proteins","volume":"123","author":"Xing","year":"2002","journal-title":"Mech. Ageing Dev."},{"key":"10.1016\/j.colsurfb.2021.112157_bib174","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1002\/(SICI)1098-2299(199604)37:4<231::AID-DDR5>3.0.CO;2-M","article-title":"Preclinical pharmacology of pramlintide in the rat: Comparisons with human and rat amylin","volume":"37","author":"Young","year":"1996","journal-title":"Drug Dev. Res."},{"key":"10.1016\/j.colsurfb.2021.112157_bib175","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1016\/j.humpath.2009.02.019","article-title":"Localized insulin-derived amyloidosis in patients with diabetes mellitus: a case report","volume":"40","author":"Yumlu","year":"2009","journal-title":"Hum. Pathol."},{"key":"10.1016\/j.colsurfb.2021.112157_bib176","doi-asserted-by":"crossref","first-page":"37721","DOI":"10.1039\/D0RA07742A","article-title":"Insulin amyloid polymorphs: implications for iatrogenic cytotoxicity","volume":"10","author":"Yuzu","year":"2020","journal-title":"RSC Adv."},{"key":"10.1016\/j.colsurfb.2021.112157_bib177","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1016\/S0140-6736(02)07952-7","article-title":"Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity, and beta-cell function in type 2 diabetes: a parallel-group study","volume":"359","author":"Zander","year":"2002","journal-title":"Lancet Lond. Engl."},{"key":"10.1016\/j.colsurfb.2021.112157_bib178","doi-asserted-by":"crossref","DOI":"10.1098\/rsfs.2017.0030","article-title":"Factors affecting the physical stability (aggregation) of peptide therapeutics","volume":"7","author":"Zapadka","year":"2017","journal-title":"Interface Focus"},{"key":"10.1016\/j.colsurfb.2021.112157_bib179","doi-asserted-by":"crossref","first-page":"16259","DOI":"10.1021\/jacs.6b05025","article-title":"A pH-induced switch in human glucagon-like peptide-1 aggregation kinetics","volume":"138","author":"Zapadka","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.colsurfb.2021.112157_bib180","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.trsl.2008.10.009","article-title":"Amyloid oligomers in diabetic and nondiabetic human pancreas","volume":"153","author":"Zhao","year":"2009","journal-title":"Transl. Res."}],"container-title":["Colloids and Surfaces B: Biointerfaces"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0927776521006019?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0927776521006019?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,15]],"date-time":"2025-10-15T11:01:12Z","timestamp":1760526072000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0927776521006019"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,1]]},"references-count":180,"alternative-id":["S0927776521006019"],"URL":"https:\/\/doi.org\/10.1016\/j.colsurfb.2021.112157","relation":{},"ISSN":["0927-7765"],"issn-type":[{"value":"0927-7765","type":"print"}],"subject":[],"published":{"date-parts":[[2022,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Amyloidogenicity of peptides targeting diabetes and obesity","name":"articletitle","label":"Article Title"},{"value":"Colloids and Surfaces B: Biointerfaces","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.colsurfb.2021.112157","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"112157"}}