Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide

Antimicrobial peptides (AMPs) selectively form pores in microbial membranes in process not fully understood. Here the authors use experimentally guided molecular dynamics to study maculatin pore formation, showing how this AMP assembles into transient and structurally diverse oligomeric pores in cel...

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Main Authors:	Yukun Wang, Charles H. Chen, Dan Hu, Martin B. Ulmschneider, Jakob P. Ulmschneider
Format:	article
Language:	EN
Published:	Nature Portfolio 2016
Subjects:	Science Q
Online Access:	https://doaj.org/article/322f5d07a3e6460aa7ea543a7dc9effb
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spelling	oai:doaj.org-article:322f5d07a3e6460aa7ea543a7dc9effb2021-12-02T17:33:10ZSpontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide10.1038/ncomms135352041-1723https://doaj.org/article/322f5d07a3e6460aa7ea543a7dc9effb2016-11-01T00:00:00Zhttps://doi.org/10.1038/ncomms13535https://doaj.org/toc/2041-1723Antimicrobial peptides (AMPs) selectively form pores in microbial membranes in process not fully understood. Here the authors use experimentally guided molecular dynamics to study maculatin pore formation, showing how this AMP assembles into transient and structurally diverse oligomeric pores in cell membranes.Yukun WangCharles H. ChenDan HuMartin B. UlmschneiderJakob P. UlmschneiderNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yukun Wang Charles H. Chen Dan Hu Martin B. Ulmschneider Jakob P. Ulmschneider Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
description	Antimicrobial peptides (AMPs) selectively form pores in microbial membranes in process not fully understood. Here the authors use experimentally guided molecular dynamics to study maculatin pore formation, showing how this AMP assembles into transient and structurally diverse oligomeric pores in cell membranes.
format	article
author	Yukun Wang Charles H. Chen Dan Hu Martin B. Ulmschneider Jakob P. Ulmschneider
author_facet	Yukun Wang Charles H. Chen Dan Hu Martin B. Ulmschneider Jakob P. Ulmschneider
author_sort	Yukun Wang
title	Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
title_short	Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
title_full	Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
title_fullStr	Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
title_full_unstemmed	Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
title_sort	spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/322f5d07a3e6460aa7ea543a7dc9effb
work_keys_str_mv	AT yukunwang spontaneousformationofstructurallydiversemembranechannelarchitecturesfromasingleantimicrobialpeptide AT charleshchen spontaneousformationofstructurallydiversemembranechannelarchitecturesfromasingleantimicrobialpeptide AT danhu spontaneousformationofstructurallydiversemembranechannelarchitecturesfromasingleantimicrobialpeptide AT martinbulmschneider spontaneousformationofstructurallydiversemembranechannelarchitecturesfromasingleantimicrobialpeptide AT jakobpulmschneider spontaneousformationofstructurallydiversemembranechannelarchitecturesfromasingleantimicrobialpeptide
_version_	1718380054386311168

Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide

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