{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,20]],"date-time":"2026-05-20T21:03:04Z","timestamp":1779310984018,"version":"3.51.4"},"reference-count":43,"publisher":"MDPI AG","issue":"18","license":[{"start":{"date-parts":[[2021,9,21]],"date-time":"2021-09-21T00:00:00Z","timestamp":1632182400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001656","name":"Helmholtz-Gemeinschaft","doi-asserted-by":"publisher","award":["BIF-TM"],"award-info":[{"award-number":["BIF-TM"]}],"id":[{"id":"10.13039\/501100001656","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["INST 121384\/58-1 FUGG"],"award-info":[{"award-number":["INST 121384\/58-1 FUGG"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001650","name":"German Academic Exchange Service New Delhi","doi-asserted-by":"publisher","award":["India IIT Master Sandwich Programme (IIT), 2018 (57434206)"],"award-info":[{"award-number":["India IIT Master Sandwich Programme (IIT), 2018 (57434206)"]}],"id":[{"id":"10.13039\/501100001650","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>A group of seven peptides from spider venom with diverse sequences constitute the latarcin family. They have been described as membrane-active antibiotics, but their lipid interactions have not yet been addressed. Using circular dichroism and solid-state 15N-NMR, we systematically characterized and compared the conformation and helix alignment of all seven peptides in their membrane-bound state. These structural results could be correlated with activity assays (antimicrobial, hemolysis, fluorescence vesicle leakage). Functional synergy was not observed amongst any of the latarcins. In the presence of lipids, all peptides fold into amphiphilic \u03b1-helices as expected, the helices being either surface-bound or tilted in the bilayer. The most tilted peptide, Ltc2a, possesses a novel kind of amphiphilic profile with a coiled-coil-like hydrophobic strip and is the most aggressive of all. It indiscriminately permeabilizes natural membranes (antimicrobial, hemolysis) as well as artificial lipid bilayers through the segregation of anionic lipids and possibly enhanced motional averaging. Ltc1, Ltc3a, Ltc4a, and Ltc5a are efficient and selective in killing bacteria but without causing significant bilayer disturbance. They act rather slowly or may even translocate towards intracellular targets, suggesting more subtle lipid interactions. Ltc6a and Ltc7, finally, do not show much antimicrobial action but can nonetheless perturb model bilayers.<\/jats:p>","DOI":"10.3390\/ijms221810156","type":"journal-article","created":{"date-parts":[[2021,9,21]],"date-time":"2021-09-21T08:04:23Z","timestamp":1632211463000},"page":"10156","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Membrane Interactions of Latarcins: Antimicrobial Peptides from Spider Venom"],"prefix":"10.3390","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7290-5154","authenticated-orcid":false,"given":"Parvesh","family":"Wadhwani","sequence":"first","affiliation":[{"name":"Institute of Biological Interfaces (IBG-2), Karlsruhe Institute of Technology (KIT), P.O. Box 3640, 76021 Karlsruhe, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Saiguru","family":"Sekaran","sequence":"additional","affiliation":[{"name":"Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, Hauz Khas, Delhi 110016, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Erik","family":"Strandberg","sequence":"additional","affiliation":[{"name":"Institute of Biological Interfaces (IBG-2), Karlsruhe Institute of Technology (KIT), P.O. Box 3640, 76021 Karlsruhe, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2256-9498","authenticated-orcid":false,"given":"Jochen","family":"B\u00fcrck","sequence":"additional","affiliation":[{"name":"Institute of Biological Interfaces (IBG-2), Karlsruhe Institute of Technology (KIT), P.O. Box 3640, 76021 Karlsruhe, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Archana","family":"Chugh","sequence":"additional","affiliation":[{"name":"Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, Hauz Khas, Delhi 110016, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5571-9483","authenticated-orcid":false,"given":"Anne S.","family":"Ulrich","sequence":"additional","affiliation":[{"name":"Institute of Biological Interfaces (IBG-2), Karlsruhe Institute of Technology (KIT), P.O. Box 3640, 76021 Karlsruhe, Germany"},{"name":"Institute of Organic Chemistry, Karlsruhe Institute of Technology (KIT), Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,9,21]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"453","DOI":"10.3389\/fcimb.2021.668632","article-title":"Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields","volume":"11","author":"Moretta","year":"2021","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Langenegger, N., Nentwig, W., and Kuhn-Nentwig, L. (2019). Spider Venom: Components, Modes of Action, and Novel Strategies in Transcriptomic and Proteomic Analyses. 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