{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T20:51:21Z","timestamp":1792270281585,"version":"4.4.0"},"reference-count":43,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"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":["Peptides"],"published-print":{"date-parts":[[2024,12]]},"DOI":"10.1016\/j.peptides.2024.171313","type":"journal-article","created":{"date-parts":[[2024,10,28]],"date-time":"2024-10-28T09:28:44Z","timestamp":1730107724000},"page":"171313","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":5,"special_numbering":"C","title":["Cm-p5, a molluscan-derived antifungal peptide exerts its activity by a membrane surface covering in a non-penetrating mode"],"prefix":"10.1016","volume":"182","author":[{"given":"M.","family":"Gonzalez-Garcia","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B.","family":"Bertrand","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"EM","family":"Martell-Huguet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"JF","family":"Espinosa-Romero","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"RF","family":"V\u00e1zquez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F.","family":"Morales \u2013Vicente","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F.","family":"Rosenau","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"LH","family":"Standker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"OL","family":"Franco","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"AJ","family":"Otero-Gonzalez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C","family":"Mu\u00f1oz-Garay","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.peptides.2024.171313_bib1","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1056\/NEJMp0804651","article-title":"Antibiotic-resistant bugs in the 21st century--a clinical super-challenge","volume":"360","author":"Arias","year":"2009","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.peptides.2024.171313_bib2","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/j.riam.2009.06.003","article-title":"Amphotericin B: side effects and toxicity","volume":"26","author":"Laniado-Labor\u00edn","year":"2009","journal-title":"Rev. Iberoam. Micol."},{"key":"10.1016\/j.peptides.2024.171313_bib3","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1128\/CMR.00029-06","article-title":"Epidemiology of invasive candidiasis: a persistent public health problem","volume":"20","author":"Pfaller","year":"2007","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.peptides.2024.171313_bib4","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.1038\/nbt1267","article-title":"Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies","volume":"24","author":"Hancock","year":"2006","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.peptides.2024.171313_bib5","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.it.2008.12.003","article-title":"AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense","volume":"30","author":"Lai","year":"2009","journal-title":"Trends Immunol."},{"key":"10.1016\/j.peptides.2024.171313_bib6","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1096\/fj.09-143388","article-title":"Antimicrobial peptides from marine invertebrates as a new frontier for microbial infection control","volume":"24","author":"Otero-Gonz\u00e1lez","year":"2010","journal-title":"FASEB J."},{"key":"10.1016\/j.peptides.2024.171313_bib7","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/j.imbio.2010.07.003","article-title":"Host defense peptides and their antimicrobial-immunomodulatory duality","volume":"216","author":"Steinstraesser","year":"2011","journal-title":"Immunobiology"},{"key":"10.1016\/j.peptides.2024.171313_bib8","doi-asserted-by":"crossref","first-page":"7738","DOI":"10.1074\/jbc.M111.303602","article-title":"Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions","volume":"287","author":"Yin","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.peptides.2024.171313_bib9","first-page":"1000e002","article-title":"Antimicrobial peptides: an emerging approach to treating colitis","volume":"1","author":"Tran","year":"2016","journal-title":"Clin. Gastroenterol. J."},{"key":"10.1016\/j.peptides.2024.171313_bib10","doi-asserted-by":"crossref","first-page":"968","DOI":"10.1016\/j.biochi.2011.12.016","article-title":"Functional characterization of a synthetic hydrophilic antifungal peptide derived from the marine snail Cenchritis muricatus","volume":"94","author":"L\u00f3pez-Abarrategui","year":"2012","journal-title":"Biochimie"},{"key":"10.1016\/j.peptides.2024.171313_bib11","doi-asserted-by":"crossref","first-page":"3315","DOI":"10.1096\/fj.14-269860","article-title":"Cm-p5: an antifungal hydrophilic peptide derived from the coastal mollusk Cenchritis muricatus (Gastropoda: Littorinidae)","volume":"29","author":"L\u00f3pez-Abarrategui","year":"2015","journal-title":"FASEB J."},{"key":"10.1016\/j.peptides.2024.171313_bib12","doi-asserted-by":"crossref","first-page":"3849","DOI":"10.2147\/IJN.S107561","article-title":"The intrinsic antimicrobial activity of citric acid-coated manganese ferrite nanoparticles is enhanced after conjugation with the antifungal peptide Cm-p5","volume":"11","author":"Lopez-Abarrategui","year":"2016","journal-title":"Int. J. Nanomed."},{"key":"10.1016\/j.peptides.2024.171313_bib13","doi-asserted-by":"crossref","first-page":"19081","DOI":"10.1021\/acsomega.9b02201","article-title":"Design of a helical-stabilized, cyclic, and nontoxic analogue of the peptide Cm-p5 with improved antifungal activity","volume":"4","author":"Vicente","year":"2019","journal-title":"ACS Omega"},{"key":"10.1016\/j.peptides.2024.171313_bib14","doi-asserted-by":"crossref","DOI":"10.3390\/antibiotics9070363","article-title":"Derivates of the antifungal peptide Cm-p5 inhibit development of biofilms in vitro","volume":"9","author":"Kubiczek","year":"2020","journal-title":"Antibiotics"},{"key":"10.1016\/j.peptides.2024.171313_bib15","doi-asserted-by":"crossref","DOI":"10.3390\/ijms24129788","article-title":"Cm-p5 peptide dimers inhibit biofilms of clinical isolates, and fluconazole-resistant mutants of","volume":"24","author":"Amann","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.peptides.2024.171313_bib16","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1016\/j.bbamem.2014.11.024","article-title":"Fungicidal mechanisms of the antimicrobial peptide Bac8c","volume":"1848","author":"Lee","year":"2015","journal-title":"Biochim Biophys. Acta"},{"key":"10.1016\/j.peptides.2024.171313_bib17","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbamem.2019.183105","article-title":"Biophysical characterization of the insertion of two potent antimicrobial peptides-Pin2 and its variant Pin2[GVG] in biological model membranes","volume":"1862","author":"Bertrand","year":"2020","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.peptides.2024.171313_bib18","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1016\/S0006-3495(90)82637-0","article-title":"Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence","volume":"57","author":"Parasassi","year":"1990","journal-title":"Biophys. J."},{"key":"10.1016\/j.peptides.2024.171313_bib19","doi-asserted-by":"crossref","DOI":"10.1038\/srep44332","article-title":"Antimicrobial peptide cWFW kills by combining lipid phase separation with autolysis","volume":"7","author":"Scheinpflug","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.peptides.2024.171313_bib20","doi-asserted-by":"crossref","first-page":"3034","DOI":"10.1016\/j.bpj.2022.07.018","article-title":"Membrane fluidity, composition, and charge affect the activity and selectivity of the AMP ascaphin-8","volume":"121","author":"Morales-Mart\u00ednez","year":"2022","journal-title":"Biophys. J."},{"key":"10.1016\/j.peptides.2024.171313_bib21","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0000880","article-title":"Automated builder and database of protein\/membrane complexes for molecular dynamics simulations","volume":"2","author":"Jo","year":"2007","journal-title":"PLoS One"},{"key":"10.1016\/j.peptides.2024.171313_bib22","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1002\/jcc.20945","article-title":"CHARMM-GUI: a web-based graphical user interface for CHARMM","volume":"29","author":"Jo","year":"2008","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.peptides.2024.171313_bib23","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1002\/jcc.21287","article-title":"CHARMM: the biomolecular simulation program","volume":"30","author":"Brooks","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.peptides.2024.171313_bib24","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1002\/jcc.23702","article-title":"CHARMM-GUI Membrane Builder toward realistic biological membrane simulations","volume":"35","author":"Wu","year":"2014","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.peptides.2024.171313_bib25","doi-asserted-by":"crossref","unstructured":"J. Lee, X. Cheng, J.M. Swails, M.S. Yeom, P.K. Eastman, J.A. Lemkul, S. Wei, J. Buckner, J.C. Jeong, Y. Qi, S. Jo, V.S. Pande, D.A. Case, C.L. Brooks III, A.D. MacKerell Jr, J.B. Klauda, W. Im, CHARMM-GUI Input Generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM\/OpenMM Simulations Using the CHARMM36 Additive Force Field, (2015). https:\/\/doi.org\/10.1021\/acs.jctc.5b00935.","DOI":"10.1021\/acs.jctc.5b00935"},{"key":"10.1016\/j.peptides.2024.171313_bib26","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1021\/ct700200b","article-title":"P-LINCS: a parallel linear constraint solver for molecular simulation","volume":"4","author":"Hess","year":"2008","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.peptides.2024.171313_bib27","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/nmeth.4067","article-title":"CHARMM36m: an improved force field for folded and intrinsically disordered proteins","volume":"14","author":"Huang","year":"2017","journal-title":"Nat. Methods"},{"key":"10.1016\/j.peptides.2024.171313_bib28","doi-asserted-by":"crossref","first-page":"3684","DOI":"10.1063\/1.448118","article-title":"Molecular dynamics with coupling to an external bath","volume":"81","author":"Berendsen","year":"1984","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.peptides.2024.171313_bib29","doi-asserted-by":"crossref","first-page":"7182","DOI":"10.1063\/1.328693","article-title":"Polymorphic transitions in single crystals: a new molecular dynamics method","volume":"52","author":"Parrinello","year":"1981","journal-title":"J. Appl. Phys."},{"key":"10.1016\/j.peptides.2024.171313_bib30","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1063\/1.447334","article-title":"A unified formulation of the constant temperature molecular dynamics methods","volume":"81","author":"Nos\u00e9","year":"1984","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.peptides.2024.171313_bib31","doi-asserted-by":"crossref","first-page":"1695","DOI":"10.1103\/PhysRevA.31.1695","article-title":"Canonical dynamics: equilibrium phase-space distributions","volume":"31","author":"Hoover","year":"1985","journal-title":"Phys. Rev. A Gen. Phys."},{"key":"10.1016\/j.peptides.2024.171313_bib32","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."},{"key":"10.1016\/j.peptides.2024.171313_bib33","doi-asserted-by":"crossref","first-page":"548","DOI":"10.6026\/97320630010548","article-title":"VMD-SS: a graphical user interface plug-in to calculate the protein secondary structure in VMD program","volume":"10","author":"Yahyavi","year":"2014","journal-title":"Bioinformation"},{"key":"10.1016\/j.peptides.2024.171313_bib34","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/S0959-440X(99)80061-X","article-title":"Lipid monolayers: why use half a membrane to characterize protein-membrane interactions?","volume":"9","author":"Brockman","year":"1999","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.peptides.2024.171313_bib35","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"},{"key":"10.1016\/j.peptides.2024.171313_bib36","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1002\/jcc.540160303","article-title":"The double cubic lattice method: efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies","volume":"16","author":"Eisenhaber","year":"1995","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.peptides.2024.171313_bib37","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/978-1-0716-1546-1_12","article-title":"Molecular dynamics simulations of protein aggregation: protocols for simulation setup and analysis with markov state models and transition networks","volume":"2340","author":"Samantray","year":"2022","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.peptides.2024.171313_bib38","doi-asserted-by":"crossref","first-page":"3884","DOI":"10.1529\/biophysj.107.107938","article-title":"Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes","volume":"93","author":"Marsh","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.peptides.2024.171313_bib39","doi-asserted-by":"crossref","first-page":"3719","DOI":"10.1038\/s41598-017-03795-6","article-title":"Interaction of the antimicrobial peptide aurein 1.2 and charged lipid bilayer","volume":"7","author":"Rai","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.peptides.2024.171313_bib40","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1590\/S0001-37652009000300015","article-title":"Antifungal and antitumor models of bioactive protective peptides","volume":"81","author":"Rodrigues","year":"2009","journal-title":"An. da Acad. Bras. De. Ci\u00ean."},{"key":"10.1016\/j.peptides.2024.171313_bib41","doi-asserted-by":"crossref","first-page":"76","DOI":"10.2174\/1568026615666150703121009","article-title":"Non-membrane permeabilizing modes of action of antimicrobial peptides on bacteria","volume":"16","author":"Scocchi","year":"2016","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.peptides.2024.171313_bib42","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1002\/pro.2449","article-title":"Contribution of hydrogen bonds to protein stability","volume":"23","author":"Pace","year":"2014","journal-title":"Protein Sci."},{"key":"10.1016\/j.peptides.2024.171313_bib43","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1021\/acs.accounts.7b00613","article-title":"Molecular dynamics simulations are redefining our view of peptides interacting with biological membranes","volume":"51","author":"Ulmschneider","year":"2018","journal-title":"Acc. Chem. Res."}],"container-title":["Peptides"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0196978124001669?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0196978124001669?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,12,12]],"date-time":"2024-12-12T18:08:23Z","timestamp":1734026903000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0196978124001669"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,12]]},"references-count":43,"alternative-id":["S0196978124001669"],"URL":"https:\/\/doi.org\/10.1016\/j.peptides.2024.171313","relation":{},"ISSN":["0196-9781"],"issn-type":[{"value":"0196-9781","type":"print"}],"subject":[],"published":{"date-parts":[[2024,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Cm-p5, a molluscan-derived antifungal peptide exerts its activity by a membrane surface covering in a non-penetrating mode","name":"articletitle","label":"Article Title"},{"value":"Peptides","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.peptides.2024.171313","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"171313"}}