Lipid-dependent pore formation by antimicrobial peptides arenicin-2 and melittin demonstrated by their proton transfer activity-Reference-Cited by-同舟云学术

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Lipid-dependent pore formation by antimicrobial peptides arenicin-2 and melittin demonstrated by their proton transfer activity

Published:2014-12-17 Issue:2 Volume:21 Page:71-76
ISSN:1075-2617
Container-title:Journal of Peptide Science
language:en
Short-container-title:J. Pept. Sci.

Author:

Sychev Sergei V.¹,Balandin Sergey V.¹,Panteleev Pavel V.¹,Barsukov Leonid I.¹,Ovchinnikova Tatiana V.¹

Affiliation:

1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry; Russian Academy of Sciences; Miklukho-Maklaya St, 16/10 117997 Moscow Russia

Publisher

Wiley

Subject

Organic Chemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,General Medicine,Biochemistry,Structural Biology

Reference50 articles.

1. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation;Matsuzaki;Biochemistry,1996

2. Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR;Hong;Structure,2006

3. Effect of lipids with different spontaneous curvature on the channel activity of colicin E1: Evidence in favor of a toroidal pore;Sobko;FEBS Lett.,2004

4. Barrel-stave model or toroidal model? A case study on melittin pores;Yang;Biophys. J.,2001

5. Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores;Allende;Biophys. J.,2005

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