Alanine scan and 2H NMR analysis of the membrane-active peptide BP100 point to a distinct carpet mechanism of action
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- 作者：Hé ; ctor Zamora-Carrerasa ; Erik Strandbergb ; Philipp Mü ; hlhä ; userb ; Jochen Bü ; rckb ; Parvesh Wadhwanib ; M. Á ; ngeles Jimé ; neza ; Marta Bruixa ; Anne S. Ulrichb ; c ; anne.ulrich@kit.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Antimicrobial peptide BP100 ; Amphipathic α-helix ; Alanine scan ; Peptide orientation and dynamics ; Lipid spontaneous curvature ; Dynamical NMR data analysis ; Geometric analysis of labeled alanines (GALA)
- 刊名：Biochimica et Biophysica Acta (BBA)-Biomembranes
- 出版年：2016
- 出版时间：June 2016
- 年：2016
- 卷：1858
- 期：6
- 页码：1328-1338
- 全文大小：1900 K
文摘
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BP100 is a short, multi-functional, membrane-active peptide.
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An Ala-scan was performed and improved therapeutic peptides identified.
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The peptide is highly helical in membranes.
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The orientation in the membrane could be determined from solid-state 2H NMR.
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BP100 membrane function is most likely based on a carpet mechanism.