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rapid analysis of molecular dynamics simulations","volume":"2016","author":"Gowers","year":"2016","journal-title":"SciPy"},{"key":"10.1016\/j.cis.2025.103775_bb0835","doi-asserted-by":"crossref","first-page":"5907","DOI":"10.1021\/acs.jctc.1c00447","article-title":"LiPyphilic: a Python toolkit for the analysis of lipid membrane simulations","volume":"17","author":"Smith","year":"2021","journal-title":"J Chem Theory Comput"},{"key":"10.1016\/j.cis.2025.103775_bb0840","doi-asserted-by":"crossref","first-page":"2118","DOI":"10.1002\/jcc.25384","article-title":"Pytim: a python package for the interfacial analysis of molecular simulations","volume":"39","author":"Sega","year":"2018","journal-title":"J Comput Chem"},{"key":"10.1016\/j.cis.2025.103775_bb0845","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1021\/acs.jcim.9b00569","article-title":"SuAVE: a tool for analyzing curvature-dependent properties in chemical interfaces","volume":"60","author":"Santos","year":"2019","journal-title":"J Chem Inf Model"},{"issue":"3","key":"10.1016\/j.cis.2025.103775_bb0850","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1007\/s00232-010-9296-8","article-title":"Lipidbook: a public repository for force-field parameters used in membrane simulations","volume":"236","author":"Doma\u0144ski","year":"2010","journal-title":"J Membr Biol"},{"key":"10.1016\/j.cis.2025.103775_bb0855","doi-asserted-by":"crossref","unstructured":"A.M. Kiirikki, H.S. Antila, L.S. Bort, P. Buslaev, F. Favela-Rosales, T.M. Ferreira, P.F.J. Fuchs, R. Garcia-Fandino, I. Gushchin, B. Kav, N. Ku\u010derka, P. Kula, M. Kurki, A. Kuzmin, A. Lalitha, F. Lolicato, J.J. Madsen, M.S. Miettinen, C. Mingham, L. Monticelli, R. Nencini, A.M. Nesterenko, T.J. Piggot, \u00c1. Pi\u00f1eiro, N. Reuter, S. Samantray, F. Su\u00e1rez-Lest\u00f3n, R. Talandashti, O.H.S. Ollila, Overlay databank unlocks data-driven analyses of biomolecules for all, Nat Commun 2024 15:1 (2024) 1136. doi: https:\/\/doi.org\/10.1038\/s41467-024-45189-z.","DOI":"10.1038\/s41467-024-45189-z"},{"key":"10.1016\/j.cis.2025.103775_bb0860","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1021\/acsphyschemau.4c00003","article-title":"Pathways to a shiny future: building the foundation for computational physical chemistry and biophysics in 2050","volume":"4","author":"Biriukov","year":"2024","journal-title":"ACS Phys Chem Au"},{"issue":"6","key":"10.1016\/j.cis.2025.103775_bb0865","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1038\/s41551-021-00689-x","article-title":"Accelerated antimicrobial discovery via deep generative models and molecular dynamics simulations","volume":"5","author":"Das","year":"2021","journal-title":"Nat Biomed Eng"},{"key":"10.1016\/j.cis.2025.103775_bb0870","article-title":"AI methods for antimicrobial peptides: progress and challenges","volume":"18","author":"Brizuela","year":"2025","journal-title":"J Microbial Biotechnol"},{"key":"10.1016\/j.cis.2025.103775_bb0875","doi-asserted-by":"crossref","DOI":"10.1016\/j.compbiomed.2024.109157","article-title":"Classical simulations on quantum computers: interface-driven peptide folding on simulated membrane surfaces","volume":"182","author":"Conde-Torres","year":"2024","journal-title":"Comput Biol Med"},{"key":"10.1016\/j.cis.2025.103775_bb0880","doi-asserted-by":"crossref","first-page":"2160","DOI":"10.1016\/j.bbamem.2014.01.016","article-title":"High-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments","volume":"1838","author":"Wang","year":"2014","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.cis.2025.103775_bb0885","doi-asserted-by":"crossref","first-page":"4318","DOI":"10.3390\/ijms24054318","article-title":"Effect of newly synthesized structures of peptides on the stability of the monolayers formed","volume":"24","author":"Golonka","year":"2023","journal-title":"Int J Mol Sci"}],"container-title":["Advances in Colloid and Interface Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0001868625003860?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0001868625003860?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,2,9]],"date-time":"2026-02-09T04:58:30Z","timestamp":1770613110000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0001868625003860"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,4]]},"references-count":177,"alternative-id":["S0001868625003860"],"URL":"https:\/\/doi.org\/10.1016\/j.cis.2025.103775","relation":{},"ISSN":["0001-8686"],"issn-type":[{"value":"0001-8686","type":"print"}],"subject":[],"published":{"date-parts":[[2026,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Antimicrobial peptides at (lipid) interfaces: Insights from monolayer models","name":"articletitle","label":"Article Title"},{"value":"Advances in Colloid and Interface Science","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cis.2025.103775","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. 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