Temperature-Dependent Transmembrane Insertion of the Amphiphilic Peptide PGLa in Lipid Bilayers Observed by Solid State 19F NMR Spectroscopy-Reference-Cited by-同舟云学术

Temperature-Dependent Transmembrane Insertion of the Amphiphilic Peptide PGLa in Lipid Bilayers Observed by Solid State 19F NMR Spectroscopy

Published:2008-11-17 Issue:49 Volume:130 Page:16512-16514
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Afonin Sergii¹,Grage Stephan L.¹,Ieronimo Marco¹,Wadhwani Parvesh¹,Ulrich Anne S.¹

Affiliation:

1. Karlsruhe Institute of Technology, Institute of Biological Interfaces, P.O. Box 3640, 76021 Karlsruhe, Germany, and Karlsruhe Institute of Technology, Institute of Organic Chemistry, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja803156d

Reference38 articles.

1. Concentration-Dependent Realignment of the Antimicrobial Peptide PGLa in Lipid Membranes Observed by Solid-State 19F-NMR

2. Conditions affecting the re-alignment of the antimicrobial peptide PGLa in membranes as monitored by solid state 2H-NMR

3. NMR methods for studying membrane-active antimicrobial peptides

4. Solid state 19F NMR methods for studying biomembranes

5. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides

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