{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T04:31:39Z","timestamp":1760243499673,"version":"build-2065373602"},"reference-count":45,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2013,7,15]],"date-time":"2013-07-15T00:00:00Z","timestamp":1373846400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>T-20 and T-1249 fusion inhibitor peptides were shown to interact  with 1-palmitoyl-2-oleyl-phosphatidylcholine (POPC) (liquid disordered, ld) and POPC\/cholesterol (1:1) (POPC\/Chol) (liquid ordered, lo) bilayers, and they do so to different extents. Although they both possess a tryptophan-rich domain (TRD), T-20 lacks a pocket binding domain (PBD), which is present in T-1249. It has been postulated that the PBD domain enhances FI interaction with HIV gp41 protein and with model membranes. Interaction of these fusion inhibitor peptides with both the cell membrane and the viral envelope membrane is important for function, i.e., inhibition of the fusion process. We address this problem with a molecular dynamics approach focusing on lipid properties, trying to ascertain the consequences and the differences in the interaction of T-20 and  T-1249 with ld and lo model membranes. T-20 and T-1249 interactions with model membranes are shown to have measurable and different effects on bilayer structural and dynamical parameters. T-1249\u2019s adsorption to the membrane surface has generally a stronger influence in the measured parameters. The presence of both binding domains in  T-1249 appears to be paramount to its stronger interaction, and is shown to have a definite importance in membrane properties upon peptide adsorption.<\/jats:p>","DOI":"10.3390\/ijms140714724","type":"journal-article","created":{"date-parts":[[2013,7,15]],"date-time":"2013-07-15T11:25:32Z","timestamp":1373887532000},"page":"14724-14743","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Effect of Amphipathic HIV Fusion Inhibitor Peptides on  POPC and POPC\/Cholesterol Membrane Properties:  A Molecular Simulation Study"],"prefix":"10.3390","volume":"14","author":[{"given":"Ant\u00f3nio","family":"Martins do Canto","sequence":"first","affiliation":[{"name":"Department of Chemistry, School of Science and Technology, University of \u00c9vora,  Rua Rom\u00e3o Ramalho, 59, 7000-671 \u00c9vora, Portugal"},{"name":"Centre for Chemistry-\u00c9vora, Rua Rom\u00e3o Ramalho, 59, 7000-671 \u00c9vora, Portugal"}]},{"given":"Alfredo","family":"Carvalho","sequence":"additional","affiliation":[{"name":"Department of Chemistry, School of Science and Technology, University of \u00c9vora,  Rua Rom\u00e3o Ramalho, 59, 7000-671 \u00c9vora, Portugal"},{"name":"Centre for Chemistry-\u00c9vora, Rua Rom\u00e3o Ramalho, 59, 7000-671 \u00c9vora, Portugal"}]},{"given":"Jo\u00e3o","family":"Ramalho","sequence":"additional","affiliation":[{"name":"Department of Chemistry, School of Science and Technology, University of \u00c9vora,  Rua Rom\u00e3o Ramalho, 59, 7000-671 \u00c9vora, Portugal"},{"name":"Centre for Chemistry-\u00c9vora, Rua Rom\u00e3o Ramalho, 59, 7000-671 \u00c9vora, Portugal"}]},{"given":"Lu\u00eds","family":"Loura","sequence":"additional","affiliation":[{"name":"Faculty of Pharmacy, University of Coimbra, Health Sciences Campus, Azinhaga de Santa Comba, 3000-548 Coimbra, Portugal"},{"name":"Centre for Chemistry-Coimbra, Rua Larga, 3004-535 Coimbra, Portugal"}]}],"member":"1968","published-online":{"date-parts":[[2013,7,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1038\/nrd1331","article-title":"Enfuvirtide: The first therapy to inhibit the entry of HIV-1 into host CD4 lymphocytes","volume":"3","author":"Matthews","year":"2004","journal-title":"Nat. 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