{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,2,3]],"date-time":"2024-02-03T00:04:32Z","timestamp":1706918672317},"reference-count":36,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2006,2,6]],"date-time":"2006-02-06T00:00:00Z","timestamp":1139184000000},"content-version":"vor","delay-in-days":36,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biopolymers"],"published-print":{"date-parts":[[2006,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The mechanism of membrane interaction by \u03b2\u2010sheet peptides is important to understand fundamental principles of folding of \u03b2\u2010barrel proteins and various \u03b2\u2010amyloid proteins. Here, we examined the conformational characteristics of a porin\u2010like channel forming (<jats:italic>x<\/jats:italic>S<jats:italic>x<\/jats:italic>G)<jats:sub>6<\/jats:sub>peptide in solution and membrane\u2010mimicking environments (CD and ATR\u2013IR) to understand the structural changes of the peptide during membrane association and channel formation. A comparison of the peptide conformations in different microenvironments showed that \u03b2\u2010sheet formation is enhanced in membrane\u2010mimicking liposomes and SDS\u2010micelles. The lipid\u2010induced \u03b2\u2010sheet formation was confirmed by the formation of a characteristic \u03b2\u2010sheet structure on mixing a methanolic solution of the peptide (partially folded) with preformed liposomes. The amphipathicity of the peptide; increased hydrogen bonding, hydrophilicity, and reduction in dimensionality of the membrane surface; membrane\u2013peptide interaction\u2013forces; and presence of flexible glycines might facilitate \u03b2\u2010sheet formation in membranes. Though the CD spectra of both the peptide\u2010bound and peptide\u2010incorporated lipids are reminiscent of a \u03b2\u2010sheet structure, a significant variation in the peak positions of the two \u03b2\u2010sheet structures was noticed. The channel characteristics of (<jats:italic>x<\/jats:italic>S<jats:italic>x<\/jats:italic>G)<jats:sub>6<\/jats:sub>in the presence of low ionic strength solutions of NEt<jats:sub>3<\/jats:sub>BzCl and glucosammonium chloride are comparable to those reported under high ionic strength solutions. Altogether the data suggest that the channel formation by (<jats:italic>x<\/jats:italic>S<jats:italic>x<\/jats:italic>G)<jats:sub>6<\/jats:sub>proceeds via \u03b2\u2010sheet aggregate formation at the membrane surface, \u03b2\u2010sheet insertion, and rearrangement into a \u03b2\u2010barrel\u2013like structure. The \u03b2\u2010barrel\u2013like channel formation most likely arises from a sequence similarity to \u03b2\u2010barrel porins whereas the lipid\u2010induced \u03b2\u2010sheet formation is governed by the above\u2010mentioned factors. \u00a9 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 317\u2013328, 2006<\/jats:p><jats:p>This article was originally published online as an accepted preprint. The \u201cPublished Online\u201d date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com<\/jats:p>","DOI":"10.1002\/bip.20470","type":"journal-article","created":{"date-parts":[[2006,2,6]],"date-time":"2006-02-06T18:48:04Z","timestamp":1139251684000},"page":"317-328","source":"Crossref","is-referenced-by-count":12,"title":["Effect of membrane mimicking environment on the conformation of a pore\u2010forming (<i>x<\/i>S<i>x<\/i>G)<sub>6<\/sub>peptide"],"prefix":"10.1002","volume":"84","author":[{"given":"Jyothi","family":"Thundimadathil","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Roger W.","family":"Roeske","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lili","family":"Guo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2006,2,6]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"crossref","first-page":"41","DOI":"10.55782\/ane-2004-1490","volume":"64","author":"Trzesniewska K.","year":"2004","journal-title":"Acta Neurobiol Exp"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00232-003-0638-7"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-4547(19990815)57:4<458::AID-JNR5>3.0.CO;2-4"},{"key":"e_1_2_6_5_2","doi-asserted-by":"crossref","first-page":"16801","DOI":"10.1016\/S0021-9258(18)55372-2","volume":"266","author":"Krantz D. 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