{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,14]],"date-time":"2026-02-14T13:40:24Z","timestamp":1771076424458,"version":"3.50.1"},"reference-count":49,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,2,1]],"date-time":"2019-02-01T00:00:00Z","timestamp":1548979200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,2,1]],"date-time":"2019-02-01T00:00:00Z","timestamp":1548979200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"name":"IITKGP"},{"DOI":"10.13039\/501100008984","name":"IIT Kharagpur","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008984","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2019,2]]},"DOI":"10.1016\/j.ijbiomac.2018.10.205","type":"journal-article","created":{"date-parts":[[2018,10,30]],"date-time":"2018-10-30T12:33:39Z","timestamp":1540902819000},"page":"20-25","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"special_numbering":"C","title":["Repulsive interaction induces fibril formation and their growth"],"prefix":"10.1016","volume":"123","author":[{"given":"Suparna","family":"Khatun","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kumari","family":"Shikha","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Agneyo","family":"Ganguly","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nisha","family":"Pawar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amar Nath","family":"Gupta","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0005","doi-asserted-by":"crossref","first-page":"3979","DOI":"10.1073\/pnas.1200506109","article-title":"Rat brains also have a default mode network","volume":"109","author":"Lu","year":"2012","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0010","doi-asserted-by":"crossref","first-page":"7763","DOI":"10.1073\/pnas.85.20.7763","article-title":"Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle","volume":"85","author":"Cooper","year":"1988","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0015","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.ijbiomac.2018.10.205_bb0020","doi-asserted-by":"crossref","first-page":"1777","DOI":"10.1002\/1873-3468.13096","article-title":"A novel amyloid designable scaffold and potential inhibitor inspired by GAIIG of amyloid beta and the HIV-1 V3 loop","volume":"592","author":"Kokotidou","year":"2018","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0025","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/0165-6147(93)90081-T","article-title":"Structure and biology of amylin","volume":"14","author":"Rink","year":"1993","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0030","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.ijbiomac.2018.10.205_bb0035","doi-asserted-by":"crossref","first-page":"19279","DOI":"10.1073\/pnas.1305517110","article-title":"Islet amyloid polypeptide toxicity and membrane interactions","volume":"110","author":"Cao","year":"2013","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0040","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/nn.3028","article-title":"The toxic A\u03b2 oligomer and Alzheimer's disease: an emperor in need of clothes","volume":"15","author":"Benilova","year":"2012","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0045","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/0141-8130(93)90039-O","article-title":"A static and dynamic light scattering study of sharp pectin fractions in aqueous solution","volume":"15","author":"Ousalem","year":"1993","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0050","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/S0022-2836(02)01175-0","article-title":"Assembly of amyloid protofibrils via critical oligomers\u2014a novel pathway of amyloid formation","volume":"325","author":"Modler","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0055","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/S0141-8130(00)00113-6","article-title":"Anomalous colloidal stability of protein coated polystyrene latex beads studied by small angle light scattering","volume":"27","author":"Bohidar","year":"2000","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0060","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1002\/cbic.200390020","article-title":"Evaluation of lipopolysaccharide aggregation by light scattering spectroscopy","volume":"4","author":"Santos","year":"2003","journal-title":"Chembiochem"},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0065","first-page":"559","article-title":"Light scattering characterization of synthetic MUC-1 peptides and their behavior in dilute solution","volume":"12","author":"Rizos","year":"2003","journal-title":"Int. J. Mol. Med."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0070","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1002\/pro.2004","article-title":"Concentration-dependent oligomerization and oligomeric arrangement of LptA","volume":"21","author":"Merten","year":"2012","journal-title":"Protein Sci."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0075","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1021\/ma00168a023","article-title":"Overlap concentration of macromolecules in solution","volume":"20","author":"Ying","year":"1987","journal-title":"Macromolecules"},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0080","series-title":"Light Scattering from Polymer Solutions","author":"Huglin","year":"1972"},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0085","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/0141-8130(88)90043-8","article-title":"Static light scattering from \u03ba-carrageenan solutions","volume":"10","author":"Slootmaekers","year":"1988","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0090","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1021\/ma00237a020","article-title":"Quasielastic light scattering of gelatin solutions and gels","volume":"16","author":"Amis","year":"1983","journal-title":"Macromolecules"},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0095","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.ijbiomac.2008.04.002","article-title":"Light scattering study of heat-denatured globular protein aggregates","volume":"43","author":"Mehalebi","year":"2008","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0100","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1093\/aob\/mcg029","article-title":"A flexible sigmoid function of determinate growth","volume":"91","author":"Yin","year":"2003","journal-title":"Ann. Bot."},{"issue":"36","key":"10.1016\/j.ijbiomac.2018.10.205_bb0105","doi-asserted-by":"crossref","first-page":"14452","DOI":"10.1073\/pnas.1206190109","article-title":"Energy landscape analysis of native folding of the prion protein yields the diffusion constant, transition path time, and rates","volume":"109","author":"Yu","year":"2012","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0110","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1038\/nchembio.131","article-title":"Amyloid formation by globular proteins under native conditions","volume":"5","author":"Chiti","year":"2009","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0115","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1021\/bi3014278","article-title":"Role of aromatic interactions in amyloid formation by islet amyloid polypeptide","volume":"52","author":"Tu","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0120","doi-asserted-by":"crossref","first-page":"6424","DOI":"10.1021\/ja710484d","article-title":"Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide","volume":"130","author":"Brender","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0125","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.bpc.2005.10.003","article-title":"Negative second virial coefficients as predictors of protein crystal growth: evidence from sedimentation equilibrium studies that refutes the designation of those light scattering parameters as osmotic virial coefficients","volume":"120","author":"Deszczynski","year":"2006","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0130","doi-asserted-by":"crossref","first-page":"2383","DOI":"10.1016\/S0006-3495(93)81312-2","article-title":"Light scattering analysis of fibril growth from the amino-terminal fragment beta (1\u201328) of beta-amyloid peptide","volume":"65","author":"Shen","year":"1993","journal-title":"Biophys. J."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0135","doi-asserted-by":"crossref","first-page":"1975","DOI":"10.1126\/science.277.5334.1975","article-title":"Enhancement of protein crystal nucleation by critical density fluctuations","volume":"277","author":"Wolde","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0140","series-title":"Methods in Enzymology","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/S0076-6879(97)76052-X","article-title":"Second virial coefficient as predictor in protein crystal growth","author":"George","year":"1997"},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0145","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1002\/ange.201508968","article-title":"Microtubule-binding R3 fragment from tau self-assembles into giant multistranded amyloid ribbons","volume":"128","author":"Adamcik","year":"2016","journal-title":"Angew. Chem."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0150","doi-asserted-by":"crossref","first-page":"2639","DOI":"10.1093\/bioinformatics\/btp449","article-title":"Enhancement of beta-sheet assembly by cooperative hydrogen bonds potential","volume":"25","author":"Levy-Moonshine","year":"2009","journal-title":"Bioinformatics"},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0155","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1006\/jmbi.1994.1334","article-title":"Satisfying hydrogen bonding potential in proteins","volume":"238","author":"McDonald","year":"1994","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0160","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1038\/nnano.2010.59","article-title":"Understanding amyloid aggregation by statistical analysis of atomic force microscopy images","volume":"5","author":"Adamcik","year":"2010","journal-title":"Nat. Nanotechnol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0165","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1039\/C0SM00502A","article-title":"Snapshots of fibrillation and aggregation kinetics in multistranded amyloid \u03b2-lactoglobulin fibrils","volume":"7","author":"Bolisetty","year":"2011","journal-title":"Soft Matter"},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0170","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.ijbiomac.2016.06.052","article-title":"Kinetics of protein fibril formation: methods and mechanisms","volume":"100","author":"Kumar","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0175","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1016\/j.ijbiomac.2017.08.080","article-title":"Strategies for optimization of heterologous protein expression in E. coli: roadblocks and reinforcements","volume":"106","author":"Kaur","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0180","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1006\/jmbi.2001.4593","article-title":"Identification of a novel human islet amyloid polypeptide \u03b2-sheet domain and factors influencing fibrillogenesis1","volume":"308","author":"Jaikaran","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0185","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.jmb.2005.02.029","article-title":"The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin","volume":"348","author":"Kajava","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0190","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1110\/ps.036509.108","article-title":"Atomic structure of the cross-\u03b2 spine of islet amyloid polypeptide (amylin)","volume":"17","author":"Wiltzius","year":"2008","journal-title":"Protein Sci."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0195","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1016\/j.jmb.2009.08.055","article-title":"Cholesterol regulates assembly of human islet amyloid polypeptide on model membranes","volume":"393","author":"Cho","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0200","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/j.jmb.2011.05.015","article-title":"A two-site mechanism for the inhibition of IAPP amyloidogenesis by zinc","volume":"410","author":"Salamekh","year":"2011","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0205","doi-asserted-by":"crossref","first-page":"12912","DOI":"10.1021\/ja504031d","article-title":"Defining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide\u2013insulin interactions","volume":"136","author":"Susa","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0210","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.abb.2017.04.005","article-title":"Ascorbic acid inhibits human insulin aggregation and protects against amyloid induced cytotoxicity","volume":"621","author":"Alam","year":"2017","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0215","doi-asserted-by":"crossref","DOI":"10.1038\/srep26759","article-title":"Vitamin k3 inhibits protein aggregation: implication in the treatment of amyloid diseases","volume":"6","author":"Alam","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0220","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1016\/j.ijbiomac.2017.03.001","article-title":"Vitamin B12 offers neuronal cell protection by inhibiting A\u03b2-42 amyloid fibrillation","volume":"99","author":"Alam","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0225","doi-asserted-by":"crossref","first-page":"311","DOI":"10.3389\/fchem.2018.00311","article-title":"Elucidating the inhibitory potential of designed peptides against amyloid fibrillation and amyloid associated cytotoxicity","volume":"6","author":"Siddiqi","year":"2018","journal-title":"Front. Chem."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0230","doi-asserted-by":"crossref","first-page":"12243","DOI":"10.1073\/pnas.91.25.12243","article-title":"Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red","volume":"91","author":"Lorenzo","year":"1994","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0235","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1002\/ana.23956","article-title":"Amylin deposition in the brain: a second amyloid in Alzheimer disease?","volume":"74","author":"Jackson","year":"2013","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0240","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1016\/j.bbadis.2014.01.002","article-title":"Exogenous amyloidogenic proteins function as seeds in amyloid \u03b2-protein aggregation","volume":"1842","author":"Ono","year":"2014","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"10.1016\/j.ijbiomac.2018.10.205_bb0245","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1038\/mp.2014.17","article-title":"Intraperitoneal injection of the pancreatic peptide amylin potently reduces behavioral impairment and brain amyloid pathology in murine models of Alzheimer's disease","volume":"20","author":"Zhu","year":"2015","journal-title":"Mol. Psychiatry"}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813018336493?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813018336493?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T07:30:37Z","timestamp":1758871837000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813018336493"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,2]]},"references-count":49,"alternative-id":["S0141813018336493"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2018.10.205","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2019,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Repulsive interaction induces fibril formation and their growth","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2018.10.205","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}