Marine antimicrobial peptide arenicin adopts a monomeric twisted β-hairpin structure and forms low conductivity pores in zwitterionic lipid bilayers-Reference-Cited by-同舟云学术

Marine antimicrobial peptide arenicin adopts a monomeric twisted β-hairpin structure and forms low conductivity pores in zwitterionic lipid bilayers

Published:2018-02-16 Issue:2 Volume:110 Page:e23093
ISSN:2475-8817
Container-title:Peptide Science
language:en
Short-container-title:Peptide Science

Author:

Sychev Sergei V.¹,Sukhanov Stanislav V.¹,Panteleev Pavel V.¹,Shenkarev Zakhar O.¹,Ovchinnikova Tatiana V.¹^ORCID

Affiliation:

1. M.M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str., 16/10; Moscow 117997 Russia

Funder

Russian Science Foundation

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,Biophysics

Reference57 articles.

1. On the design of supramolecular assemblies made of peptides and lipid bilayers

2. Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaetaArenicola marina

3. Recombinant expression, synthesis, purification, and solution structure of arenicin

4. Structure and mode of action of the antimicrobial peptide arenicin

5. Molecular dynamics simulation of antimicrobial peptide arenicin-2: β-Hairpin stabilization by noncovalent interactions

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