Melittin can permeabilize membranes via large transient pores-Reference-Cited by-同舟云学术

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Melittin can permeabilize membranes via large transient pores

Published:2024-08-23 Issue:1 Volume:15 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Ulmschneider Jakob P.^ORCID,Ulmschneider Martin B.^ORCID

Funder

National Science Foundation of China | National Natural Science Foundation of China-Yunnan Joint Fund

Natural Science Foundation of Shanghai

Shanghai Science and Technology Development Foundation

RCUK | Biotechnology and Biological Sciences Research Council

Publisher

Springer Science and Business Media LLC

Link

https://www.nature.com/articles/s41467-024-51691-1.pdf

Reference115 articles.

1. Bayley, H. Designed membrane channels and pores. Curr. Opin. Biotechnol. 10, 94–103 (1999).

2. Hancock, R. E. W. & Sahl, H.-G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24, 1551–1557 (2006).

3. Sani, M.-A. & Separovic, F. How membrane-active peptides get into lipid membranes. Acc. Chem. Res. 49, 1130–1138 (2016).

4. Guha, S., Ghimire, J., Wu, E. & Wimley, W. C. Mechanistic landscape of membrane-permeabilizing peptides. Chem. Rev. https://www.ncbi.nlm.nih.gov/pubmed/30624911 (2019).

5. Perrin, B. S. J. & Pastor, R. W. Simulations of membrane-disrupting peptides I: Alamethicin pore stability and spontaneous insertion. Biophys. J. 111, 1248–1257 (2016).

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