{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,19]],"date-time":"2026-10-19T17:22:15Z","timestamp":1792430535036,"version":"4.5.0"},"reference-count":89,"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"}],"funder":[{"DOI":"10.13039\/501100000266","name":"Engineering and Physical Sciences Research Council","doi-asserted-by":"publisher","award":["EP\/N007174\/1"],"award-info":[{"award-number":["EP\/N007174\/1"]}],"id":[{"id":"10.13039\/501100000266","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000266","name":"Engineering and Physical Sciences Research Council","doi-asserted-by":"publisher","award":["EP\/N023579\/1"],"award-info":[{"award-number":["EP\/N023579\/1"]}],"id":[{"id":"10.13039\/501100000266","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000288","name":"Royal Society","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000288","id-type":"DOI","asserted-by":"publisher"}]}],"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.2021.112165","type":"journal-article","created":{"date-parts":[[2021,10,21]],"date-time":"2021-10-21T21:58:23Z","timestamp":1634853503000},"page":"112165","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":31,"special_numbering":"P2","title":["Correlation between the secondary structure and surface activity of \u03b2-sheet forming cationic amphiphilic peptides and their anticancer activity"],"prefix":"10.1016","volume":"209","author":[{"given":"Roja","family":"Hadianamrei","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mhd Anas","family":"Tomeh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7581-7491","authenticated-orcid":false,"given":"Stephen","family":"Brown","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiqian","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4620-2893","authenticated-orcid":false,"given":"Xiubo","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"7239","key":"10.1016\/j.colsurfb.2021.112165_bib1","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1038\/nature07943","article-title":"The cancer genome","volume":"458","author":"Stratton","year":"2009","journal-title":"Nature"},{"issue":"10","key":"10.1016\/j.colsurfb.2021.112165_bib2","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1038\/s41568-020-0290-x","article-title":"A compendium of mutational cancer driver genes","volume":"20","author":"Mart\u00ednez-Jim\u00e9nez","year":"2020","journal-title":"Nat. Rev. Cancer"},{"issue":"7637","key":"10.1016\/j.colsurfb.2021.112165_bib3","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1038\/nature21349","article-title":"Elements of cancer immunity and the cancer\u2013immune set point","volume":"541","author":"Chen","year":"2017","journal-title":"Nature"},{"issue":"5","key":"10.1016\/j.colsurfb.2021.112165_bib4","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1016\/j.cell.2011.02.013","article-title":"Hallmarks of cancer: the next generation","volume":"144","author":"Hanahan","year":"2011","journal-title":"Cell"},{"issue":"2","key":"10.1016\/j.colsurfb.2021.112165_bib5","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.critrevonc.2012.03.002","article-title":"Cancer chemotherapy: a critical analysis of its 60 years of history","volume":"84","author":"Galmarini","year":"2012","journal-title":"Crit. Rev. Oncol.\/Hematol."},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib6","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1038\/ki.2012.484","article-title":"Glomerular diseases seen with cancer and chemotherapy: a narrative review","volume":"84","author":"Jhaveri","year":"2013","journal-title":"Kidney Intern."},{"issue":"2","key":"10.1016\/j.colsurfb.2021.112165_bib7","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1007\/s40264-014-0258-4","article-title":"Cancer chemotherapy and cardiac arrhythmias: a review","volume":"38","author":"Tamargo","year":"2015","journal-title":"Drug Safety"},{"issue":"4","key":"10.1016\/j.colsurfb.2021.112165_bib8","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1002\/pon.1245","article-title":"Chemotherapy-induced alopecia and effects on quality of life among women with breast cancer: a literature review","volume":"17","author":"Lemieux","year":"2008","journal-title":"Psycho-Oncol."},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib9","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1007\/s10549-007-9706-5","article-title":"Depression, quality of life and breast cancer: a review of the literature","volume":"110","author":"Reich","year":"2008","journal-title":"Breast Cancer Res. Treat."},{"issue":"12","key":"10.1016\/j.colsurfb.2021.112165_bib10","doi-asserted-by":"crossref","first-page":"1519","DOI":"10.1002\/bjs.5525","article-title":"Late adverse effects of short\u2010course preoperative radiotherapy in rectal cancer","volume":"93","author":"Pollack","year":"2006","journal-title":"Br. J. Surg."},{"issue":"2","key":"10.1016\/j.colsurfb.2021.112165_bib11","doi-asserted-by":"crossref","DOI":"10.1158\/2159-8290.CD-13-0197","article-title":"Radiogenomics: using genetics to identify cancer patients at risk for development of adverse effects following radiotherapy","volume":"4","author":"Kerns","year":"2014","journal-title":"Cancer Discov."},{"issue":"19","key":"10.1016\/j.colsurfb.2021.112165_bib12","doi-asserted-by":"crossref","DOI":"10.1158\/1078-0432.CCR-08-0700","article-title":"Single nucleotide polymorphisms, apoptosis, and the development of severe late adverse effects after radiotherapy","volume":"14","author":"Azria","year":"2008","journal-title":"Clin. Cancer Res."},{"issue":"6","key":"10.1016\/j.colsurfb.2021.112165_bib13","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1016\/j.ctrv.2007.07.011","article-title":"Cardiovascular effects of breast cancer radiotherapy","volume":"33","author":"Senkus-Konefka","year":"2007","journal-title":"Cancer Treat. Rev."},{"issue":"12","key":"10.1016\/j.colsurfb.2021.112165_bib14","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1038\/s41568-020-00302-4","article-title":"Non-genetic mechanisms of therapeutic resistance in cancer","volume":"20","author":"Marine","year":"2020","journal-title":"Nat. Rev. Cancer"},{"issue":"4","key":"10.1016\/j.colsurfb.2021.112165_bib15","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1038\/nrc3236","article-title":"Antibody therapy of cancer","volume":"12","author":"Scott","year":"2012","journal-title":"Nat. Rev. Cancer"},{"issue":"7","key":"10.1016\/j.colsurfb.2021.112165_bib16","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1038\/nrd.2018.75","article-title":"The promise and challenges of immune agonist antibody development in cancer","volume":"17","author":"Mayes","year":"2018","journal-title":"Nat. Rev. Drug Discov."},{"issue":"8","key":"10.1016\/j.colsurfb.2021.112165_bib17","doi-asserted-by":"crossref","first-page":"681","DOI":"10.2217\/imt-2017-0024","article-title":"The future of immune checkpoint cancer therapy after PD-1 and CTLA-4","volume":"9","author":"Hahn","year":"2017","journal-title":"Immunotherapy"},{"issue":"12","key":"10.1016\/j.colsurfb.2021.112165_bib18","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1038\/s41571-020-0413-z","article-title":"Immunostimulation with chemotherapy in the era of immune checkpoint inhibitors","volume":"17","author":"Galluzzi","year":"2020","journal-title":"Nat. Rev. Clin. Oncol."},{"issue":"4","key":"10.1016\/j.colsurfb.2021.112165_bib19","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/j.ccell.2016.03.005","article-title":"Tumoral immune cell exploitation in colorectal cancer metastases can be targeted effectively by anti-CCR5 therapy in cancer patients","volume":"29","author":"Halama","year":"2016","journal-title":"Cancer Cell"},{"issue":"6","key":"10.1016\/j.colsurfb.2021.112165_bib20","doi-asserted-by":"crossref","first-page":"1466","DOI":"10.1172\/JCI32446","article-title":"Adoptive T cell therapy for cancer in the clinic","volume":"117","author":"June","year":"2007","journal-title":"J. Clin. Investig."},{"key":"10.1016\/j.colsurfb.2021.112165_bib21","doi-asserted-by":"crossref","first-page":"176","DOI":"10.3389\/fonc.2019.00176","article-title":"The emergence of universal immune receptor T cell therapy for cancer","volume":"9","author":"Minutolo","year":"2019","journal-title":"Front. Oncol."},{"issue":"5","key":"10.1016\/j.colsurfb.2021.112165_bib22","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1038\/nri2744","article-title":"Monoclonal antibodies: versatile platforms for cancer immunotherapy","volume":"10","author":"Weiner","year":"2010","journal-title":"Nat. Rev. Immunol."},{"issue":"9668","key":"10.1016\/j.colsurfb.2021.112165_bib23","doi-asserted-by":"crossref","first-page":"1033","DOI":"10.1016\/S0140-6736(09)60251-8","article-title":"Monoclonal antibodies for cancer immunotherapy","volume":"373","author":"Weiner","year":"2009","journal-title":"Lancet"},{"issue":"5","key":"10.1016\/j.colsurfb.2021.112165_bib24","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1038\/nrd.2017.84","article-title":"CAR T therapies drive into new terrain","volume":"16","author":"Kingwell","year":"2017","journal-title":"Nat. Rev. Drug Discov."},{"issue":"12","key":"10.1016\/j.colsurfb.2021.112165_bib25","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1634\/theoncologist.12-12-1443","article-title":"Review: side effects of approved molecular targeted therapies in solid cancers","volume":"12","author":"Widakowich","year":"2007","journal-title":"Oncologist"},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib26","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.critrevonc.2004.10.011","article-title":"Overview of monoclonal antibodies in cancer therapy: present and promise","volume":"54","author":"Stern","year":"2005","journal-title":"Crit. Rev. Oncol.\/Hematol."},{"issue":"4","key":"10.1016\/j.colsurfb.2021.112165_bib27","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1038\/nrclinonc.2015.213","article-title":"Kinase inhibitors and monoclonal antibodies in oncology: clinical implications","volume":"13","author":"Gharwan","year":"2016","journal-title":"Nat. Rev. Clin. Oncol."},{"issue":"4","key":"10.1016\/j.colsurfb.2021.112165_bib28","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1038\/nrd3003","article-title":"The safety and side effects of monoclonal antibodies","volume":"9","author":"Hansel","year":"2010","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.colsurfb.2021.112165_bib29","first-page":"151","author":"Pichler","year":"2007","journal-title":"Adverse Side Effects to Biological Agents"},{"key":"10.1016\/j.colsurfb.2021.112165_bib30","doi-asserted-by":"crossref","DOI":"10.1136\/bmj.e8346","article-title":"Monoclonal antibodies: magic bullets with a hefty price tag","volume":"345","author":"Shaughnessy","year":"2012","journal-title":"BMJ: Br. Med. J."},{"key":"10.1016\/j.colsurfb.2021.112165_bib31","doi-asserted-by":"crossref","first-page":"193","DOI":"10.3389\/fphar.2016.00193","article-title":"Overcoming barriers to the market access of biosimilars in the European Union: the case of biosimilar monoclonal antibodies","volume":"7","author":"Moorkens","year":"2016","journal-title":"Front. Pharmacol."},{"issue":"28","key":"10.1016\/j.colsurfb.2021.112165_bib32","doi-asserted-by":"crossref","first-page":"46635","DOI":"10.18632\/oncotarget.16743","article-title":"Antimicrobial peptides with selective antitumor mechanisms: prospect for anticancer applications","volume":"8","author":"Deslouches","year":"2017","journal-title":"Oncotarget"},{"key":"10.1016\/j.colsurfb.2021.112165_bib33","doi-asserted-by":"crossref","first-page":"5","DOI":"10.3389\/fchem.2017.00005","article-title":"Peptides with dual antimicrobial and anticancer activities","volume":"5","author":"Fel\u00edcio","year":"2017","journal-title":"Front. Chem."},{"key":"10.1016\/j.colsurfb.2021.112165_bib34","doi-asserted-by":"crossref","first-page":"294","DOI":"10.3389\/fmicb.2013.00294","article-title":"From antimicrobial to anticancer peptides. A review","volume":"4","author":"Gaspar","year":"2013","journal-title":"Front. Microbiol."},{"issue":"8","key":"10.1016\/j.colsurfb.2021.112165_bib35","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1016\/j.chemphyslip.2011.09.004","article-title":"Membrane-active host defense peptides \u2013 Challenges and perspectives for the development of novel anticancer drugs","volume":"164","author":"Riedl","year":"2011","journal-title":"Chem. Phys. Lipids"},{"issue":"2","key":"10.1016\/j.colsurfb.2021.112165_bib36","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/j.bbamem.2007.11.008","article-title":"Studies on anticancer activities of antimicrobial peptides","volume":"1778","author":"Hoskin","year":"2008","journal-title":"Biochim. Biophys. Acta ((BBA)) - Biomembr."},{"key":"10.1016\/j.colsurfb.2021.112165_bib37","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.cocis.2018.06.009","article-title":"Membrane interactions and cell selectivity of amphiphilic anticancer peptides","volume":"38","author":"Nystr\u00f6m","year":"2018","journal-title":"Curr. Opin. Colloid Interface Sci."},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib38","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.canlet.2014.05.002","article-title":"Peptide-based cancer therapy: opportunity and challenge","volume":"351","author":"Wu","year":"2014","journal-title":"Cancer Lett."},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib39","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/j.ejphar.2009.08.043","article-title":"Cationic amphiphilic peptides with cancer-selective toxicity","volume":"625","author":"Schweizer","year":"2009","journal-title":"Eur. J. Pharmacol."},{"issue":"38","key":"10.1016\/j.colsurfb.2021.112165_bib40","doi-asserted-by":"crossref","first-page":"34609","DOI":"10.1021\/acsami.9b10028","article-title":"Hydrophobic control of the bioactivity and cytotoxicity of de novo-designed antimicrobial peptides","volume":"11","author":"Gong","year":"2019","journal-title":"ACS Appl. Mater. Interfaces"},{"issue":"40","key":"10.1016\/j.colsurfb.2021.112165_bib41","doi-asserted-by":"crossref","first-page":"26501","DOI":"10.1021\/acsami.6b08297","article-title":"Surface physical activity and hydrophobicity of designed helical peptide amphiphiles control their bioactivity and cell selectivity","volume":"8","author":"Chen","year":"2016","journal-title":"ACS Appl. Mater. Interfaces"},{"issue":"13","key":"10.1016\/j.colsurfb.2021.112165_bib42","doi-asserted-by":"crossref","DOI":"10.1007\/s00018-011-0710-x","article-title":"Multifunctional cationic host defence peptides and their clinical applications","volume":"68","author":"Yeung","year":"2011","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.colsurfb.2021.112165_bib43","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.addr.2014.10.013","article-title":"Strategies employed in the design and optimization of synthetic antimicrobial peptide amphiphiles with enhanced therapeutic potentials","volume":"78","author":"Ong","year":"2014","journal-title":"Adv. Drug Deliv. Rev."},{"issue":"5","key":"10.1016\/j.colsurfb.2021.112165_bib44","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1007\/s00894-019-4007-6","article-title":"De novo design of anticancer peptides by ensemble artificial neural networks","volume":"25","author":"Grisoni","year":"2019","journal-title":"J. Mol. Model."},{"issue":"35","key":"10.1016\/j.colsurfb.2021.112165_bib45","doi-asserted-by":"crossref","first-page":"10370","DOI":"10.1002\/anie.201504018","article-title":"Multidimensional design of anticancer peptides","volume":"54","author":"Lin","year":"2015","journal-title":"Angew. Chem. Intern. Ed."},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib46","doi-asserted-by":"crossref","first-page":"2984","DOI":"10.1038\/srep02984","article-title":"In silico models for designing and discovering novel anticancer peptides","volume":"3","author":"Tyagi","year":"2013","journal-title":"Sci. Rep."},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib47","doi-asserted-by":"crossref","first-page":"11282","DOI":"10.1038\/s41598-019-47568-9","article-title":"In silico design and optimization of selective membranolytic anticancer peptides","volume":"9","author":"Gabernet","year":"2019","journal-title":"Sci. Rep."},{"issue":"9","key":"10.1016\/j.colsurfb.2021.112165_bib48","doi-asserted-by":"crossref","first-page":"1436","DOI":"10.1016\/j.bbamem.2006.03.021","article-title":"Alpha-helical antimicrobial peptides\u2014Using a sequence template to guide structure\u2013activity relationship studies","volume":"1758","author":"Zelezetsky","year":"2006","journal-title":"Biochim. Biophys. Acta ((BBA)) - Biomembr."},{"issue":"29","key":"10.1016\/j.colsurfb.2021.112165_bib49","doi-asserted-by":"crossref","first-page":"3682","DOI":"10.1002\/adfm.201202850","article-title":"Short synthetic \u03b2-sheet forming peptide amphiphiles as broad spectrum antimicrobials with antibiofilm and endotoxin neutralizing capabilities","volume":"23","author":"Ong","year":"2013","journal-title":"Adv. Funct. Mater."},{"issue":"4","key":"10.1016\/j.colsurfb.2021.112165_bib50","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1016\/j.biomaterials.2013.10.053","article-title":"Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic \u03b2-sheet forming peptide amphiphiles","volume":"35","author":"Ong","year":"2014","journal-title":"Biomaterials"},{"key":"10.1016\/j.colsurfb.2021.112165_bib51","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.biomaterials.2014.11.052","article-title":"Synthetic \u03b2-sheet forming peptide amphiphiles for treatment of fungal keratitis","volume":"43","author":"Wu","year":"2015","journal-title":"Biomaterials"},{"issue":"2","key":"10.1016\/j.colsurfb.2021.112165_bib52","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1016\/j.biomaterials.2011.09.059","article-title":"Molecular mechanisms of antibacterial and antitumor actions of designed surfactant-like peptides","volume":"33","author":"Chen","year":"2012","journal-title":"Biomaterials"},{"key":"10.1016\/j.colsurfb.2021.112165_bib53","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/j.cis.2017.06.001","article-title":"The interaction of antimicrobial peptides with membranes","volume":"247","author":"Travkova","year":"2017","journal-title":"Adv. Colloid Interface Sci."},{"issue":"7","key":"10.1016\/j.colsurfb.2021.112165_bib54","doi-asserted-by":"crossref","first-page":"2080","DOI":"10.1021\/mp300167e","article-title":"Rational development of a cytotoxic peptide to trigger cell death","volume":"9","author":"Boohaker","year":"2012","journal-title":"Mol. Pharm."},{"issue":"2","key":"10.1016\/j.colsurfb.2021.112165_bib55","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1110\/ps.29402","article-title":"Toward genomic identification of \u03b2-barrel membrane proteins: composition and architecture of known structures","volume":"11","author":"Wimley","year":"2002","journal-title":"Protein Sci."},{"issue":"18","key":"10.1016\/j.colsurfb.2021.112165_bib56","doi-asserted-by":"crossref","first-page":"5510","DOI":"10.1021\/bi00184a020","article-title":"A thermodynamic scale for the.beta.-sheet forming tendencies of the amino acids","volume":"33","author":"Smith","year":"1994","journal-title":"Biochemistry"},{"issue":"6464","key":"10.1016\/j.colsurfb.2021.112165_bib57","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1038\/367660a0","article-title":"Measurement of the \u03b2-sheet-forming propensities of amino acids","volume":"367","author":"Minor","year":"1994","journal-title":"Nature"},{"issue":"6417","key":"10.1016\/j.colsurfb.2021.112165_bib58","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/362267a0","article-title":"Thermodynamic \u03b2 -sheet propensities measured using a zinc-finger host peptide","volume":"362","author":"Kim","year":"1993","journal-title":"Nature"},{"issue":"7","key":"10.1016\/j.colsurfb.2021.112165_bib59","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1002\/pro.5560050709","article-title":"A recipe for designing water-soluble, \u03b2-sheet-forming peptides","volume":"5","author":"Mayo","year":"1996","journal-title":"Protein Sci."},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib60","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1007\/s11010-009-0172-8","article-title":"The effect of C-terminal amidation on the efficacy and selectivity of antimicrobial and anticancer peptides","volume":"332","author":"Dennison","year":"2009","journal-title":"Mol. Cell. Biochem."},{"issue":"5","key":"10.1016\/j.colsurfb.2021.112165_bib61","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1016\/j.biomaterials.2013.10.082","article-title":"Molecular mechanisms of anticancer action and cell selectivity of short \u03b1-helical peptides","volume":"35","author":"Chen","year":"2014","journal-title":"Biomaterials"},{"issue":"31","key":"10.1016\/j.colsurfb.2021.112165_bib62","doi-asserted-by":"crossref","first-page":"17346","DOI":"10.1021\/acsami.5b04547","article-title":"High selective performance of designed antibacterial and anticancer peptide amphiphiles","volume":"7","author":"Chen","year":"2015","journal-title":"ACS Appl. Mater. Interfaces"},{"issue":"5881","key":"10.1016\/j.colsurfb.2021.112165_bib63","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1038\/299371a0","article-title":"The helical hydrophobic moment: a measure of the amphiphilicity of a helix","volume":"299","author":"Eisenberg","year":"1982","journal-title":"Nature"},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib64","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/0022-2836(84)90309-7","article-title":"Analysis of membrane and surface protein sequences with the hydrophobic moment plot","volume":"179","author":"Eisenberg","year":"1984","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2021.112165_bib65","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/S0021-9673(00)82337-7","article-title":"Partition coefficients of amino acids and hydrophobic parameters \u03c0 of their side-chains as measured by thin-layer chromatography","volume":"216","author":"Pli\u0161ka","year":"1981","journal-title":"J. Chromatogr. A"},{"issue":"4","key":"10.1016\/j.colsurfb.2021.112165_bib66","first-page":"7","article-title":"Hydrophobic parameters \u03a0 of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides","volume":"18","author":"Fauch\u00e8re","year":"1983","journal-title":"Eur. J. Med. Chem."},{"issue":"8","key":"10.1016\/j.colsurfb.2021.112165_bib67","doi-asserted-by":"crossref","first-page":"2204","DOI":"10.1016\/j.biomaterials.2010.11.054","article-title":"Synthetic cationic amphiphilic \u03b1-helical peptides as antimicrobial agents","volume":"32","author":"Wiradharma","year":"2011","journal-title":"Biomaterials"},{"key":"10.1016\/j.colsurfb.2021.112165_bib68","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.actbio.2015.09.015","article-title":"Designing \u03b1-helical peptides with enhanced synergism and selectivity against mycobacterium smegmatis: discerning the role of hydrophobicity and helicity","volume":"28","author":"Khara","year":"2015","journal-title":"Acta Biomater."},{"key":"10.1016\/j.colsurfb.2021.112165_bib69","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1016\/j.colsurfb.2016.02.003","article-title":"Role of amphipathicity and hydrophobicity in the balance between hemolysis and peptide\u2013membrane interactions of three related antimicrobial peptides","volume":"141","author":"Hollmann","year":"2016","journal-title":"Colloids Surf. B: Biointerfaces"},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib70","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/S0005-2736(99)00203-5","article-title":"The monolayer technique: a potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes","volume":"1462","author":"Maget-Dana","year":"1999","journal-title":"Biochim. Biophys. Acta ((BBA)) - Biomembr."},{"issue":"11","key":"10.1016\/j.colsurfb.2021.112165_bib71","doi-asserted-by":"crossref","first-page":"7482","DOI":"10.1021\/acsomega.7b01270","article-title":"Influence of acyl chain saturation on the membrane-binding activity of a short antimicrobial peptide","volume":"2","author":"Ciumac","year":"2017","journal-title":"ACS Omega"},{"issue":"11","key":"10.1016\/j.colsurfb.2021.112165_bib72","doi-asserted-by":"crossref","first-page":"2050","DOI":"10.1016\/j.peptides.2005.04.007","article-title":"Correlation between the activities of \u03b1-helical antimicrobial peptides and hydrophobicities represented as RP HPLC retention times","volume":"26","author":"Kim","year":"2005","journal-title":"Peptides"},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib73","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/S0006-3495(95)80194-3","article-title":"Induced conformational states of amphipathic peptides in aqueous\/lipid environments","volume":"68","author":"Blondelle","year":"1995","journal-title":"Biophys. J."},{"issue":"6","key":"10.1016\/j.colsurfb.2021.112165_bib74","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1016\/j.bbamem.2010.03.005","article-title":"Secondary structure of cell-penetrating peptides controls membrane interaction and insertion","volume":"1798","author":"Eir\u00edksd\u00f3ttir","year":"2010","journal-title":"Biochim. Biophys. Acta ((BBA)) - Biomembr."},{"issue":"16","key":"10.1016\/j.colsurfb.2021.112165_bib75","doi-asserted-by":"crossref","first-page":"5109","DOI":"10.1021\/bi9600153","article-title":"Solvation energies of amino acid side chains and backbone in a family of host\u2212guest pentapeptides","volume":"35","author":"Wimley","year":"1996","journal-title":"Biochemistry"},{"issue":"8","key":"10.1016\/j.colsurfb.2021.112165_bib76","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1093\/protein\/15.8.659","article-title":"Quantifying the accessible surface area of protein residues in their local environment","volume":"15","author":"Samanta","year":"2002","journal-title":"Protein Eng., Design Sel."},{"issue":"6","key":"10.1016\/j.colsurfb.2021.112165_bib77","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1080\/07391102.2001.10506715","article-title":"Electronic properties of the amino acid side chains contribute to the structural preferences in protein folding","volume":"18","author":"Dwyer","year":"2001","journal-title":"J. Biomol. Struct. Dyn."},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib78","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/1472-6769-5-2","article-title":"Electronic properties of amino acid side chains: quantum mechanics calculation of substituent effects","volume":"5","author":"Dwyer","year":"2005","journal-title":"BMC Chem. Biol."},{"issue":"22","key":"10.1016\/j.colsurfb.2021.112165_bib79","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.96.22.12494","article-title":"Measures of residue density in protein structures","volume":"96","author":"Baud","year":"1999","journal-title":"Proceed. Natl. Acad. Sci."},{"issue":"46","key":"10.1016\/j.colsurfb.2021.112165_bib80","doi-asserted-by":"crossref","first-page":"12946","DOI":"10.1073\/pnas.1616138113","article-title":"Characterizing hydrophobicity of amino acid side chains in a protein environment via measuring contact angle of a water nanodroplet on planar peptide network","volume":"113","author":"Zhu","year":"2016","journal-title":"Proceed. Natl. Acad. Sci."},{"issue":"3","key":"10.1016\/j.colsurfb.2021.112165_bib81","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/S0968-5677(97)00017-5","article-title":"Amphiphilic peptides as models for protein-membrane interactions: interfacial behaviour of sequential Lys- and Leu-based peptides and their penetration into lipid monolayers","volume":"4","author":"Maget-Dana","year":"1997","journal-title":"Supramol. Sci."},{"key":"10.1016\/j.colsurfb.2021.112165_bib82","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/j.colsurfb.2016.10.043","article-title":"Implications of lipid monolayer charge characteristics on their selective interactions with a short antimicrobial peptide","volume":"150","author":"Ciumac","year":"2017","journal-title":"Colloids Surf. B: Biointerfaces"},{"issue":"14","key":"10.1016\/j.colsurfb.2021.112165_bib83","doi-asserted-by":"crossref","first-page":"2184","DOI":"10.1002\/smll.201102413","article-title":"Self-assembling peptide-based nanoparticles for siRNA delivery in primary cell lines","volume":"8","author":"Deshayes","year":"2012","journal-title":"Small"},{"issue":"16","key":"10.1016\/j.colsurfb.2021.112165_bib84","doi-asserted-by":"crossref","first-page":"3880","DOI":"10.1021\/acs.jpcb.6b01558","article-title":"Binding of the cationic peptide (KL)4K to lipid monolayers at the air\u2013water interface: effect of lipid headgroup charge, acyl chain length, and acyl chain saturation","volume":"120","author":"H\u00e4dicke","year":"2016","journal-title":"J. Phys. Chem. B"},{"issue":"9","key":"10.1016\/j.colsurfb.2021.112165_bib85","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.88.9.3671","article-title":"Intracellular heterogeneity in mitochondrial membrane potentials revealed by a J-aggregate-forming lipophilic cation JC-1","volume":"88","author":"Smiley","year":"1991","journal-title":"Proceed. Natl. Acad. Sci."},{"issue":"18","key":"10.1016\/j.colsurfb.2021.112165_bib86","doi-asserted-by":"crossref","first-page":"4480","DOI":"10.1021\/bi00232a015","article-title":"J-aggregate formation of a carbocyanine as a quantitative fluorescent indicator of membrane potential","volume":"30","author":"Reers","year":"1991","journal-title":"Biochemistry"},{"issue":"2","key":"10.1016\/j.colsurfb.2021.112165_bib87","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1083\/jcb.138.2.449","article-title":"Mitochondrial proliferation and paradoxical membrane depolarization during terminal differentiation and apoptosis in a human colon carcinoma cell line","volume":"138","author":"Mancini","year":"1997","journal-title":"J. Cell Biol."},{"issue":"1","key":"10.1016\/j.colsurfb.2021.112165_bib88","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1006\/excr.1998.4245","article-title":"Role of mitochondrial membrane potential in concanavalin a-induced apoptosis in human fibroblasts","volume":"245","author":"Kulkarni","year":"1998","journal-title":"Exp. Cell Res."},{"issue":"4","key":"10.1016\/j.colsurfb.2021.112165_bib89","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1128\/AAC.00925-06","article-title":"Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides","volume":"51","author":"Chen","year":"2007","journal-title":"Antimicrob. Agents Chemother."}],"container-title":["Colloids and Surfaces B: Biointerfaces"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0927776521006093?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0927776521006093?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,15]],"date-time":"2025-10-15T11:01:49Z","timestamp":1760526109000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0927776521006093"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,1]]},"references-count":89,"alternative-id":["S0927776521006093"],"URL":"https:\/\/doi.org\/10.1016\/j.colsurfb.2021.112165","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":"Correlation between the secondary structure and surface activity of \u03b2-sheet forming cationic amphiphilic peptides and their anticancer activity","name":"articletitle","label":"Article Title"},{"value":"Colloids and Surfaces B: Biointerfaces","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.colsurfb.2021.112165","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":"112165"}}