Gramicidin A disassembles large conductive clusters of its lysine-substituted derivatives in lipid membranes-Reference-Cited by-同舟云学术

Gramicidin A disassembles large conductive clusters of its lysine-substituted derivatives in lipid membranes

Published:2015 Issue:26 Volume:17 Page:17461-17470
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Antonenko Yuri N.¹²³⁴,S. Gluhov Grigory⁵⁶²⁷⁴,M. Firsov Alexander¹²³⁴,D. Pogozheva Irina⁸⁹¹⁰¹¹,Kovalchuk Sergey I.¹²¹³⁷⁴,V. Pechnikova Evgeniya¹⁴¹³⁷⁴,Kotova Elena A.¹²³⁴,S. Sokolova Olga⁵⁶²⁷⁴

Affiliation:

1. Belozersky Institute of Physico-Chemical Biology

2. Lomonosov Moscow State University

3. Moscow 119991

4. Russia

5. Department of Bioengineering

6. Faculty of Biology

7. Moscow

8. Department of Medicinal Chemistry

9. University of Michigan

10. Ann Arbor

11. USA

12. M.M. Shemyakin and Y.A. Ovchinnikov Institute of Bioorganic Chemistry

13. Russian Academy of Sciences

14. A.V.Shoubnikov Institute of Crystallography

Abstract

Gramicidin A (gA) blocks dye leakage from liposomes induced by [Lys3]gA, thereby highlighting the importance of cation–π interactions for pore formation. Based on cryo-em, large pores are attributed to 40 Å-diameter peptide clusters.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2015/CP/C5CP02047F

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