Histidine-Mediated Ion Specific Effects Enable Salt Tolerance of a Pore-Forming Marine Antimicrobial Peptide.


Journal

Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543

Informations de publication

Date de publication:
20 06 2022
Historique:
received: 25 06 2021
pubmed: 31 3 2022
medline: 15 6 2022
entrez: 30 3 2022
Statut: ppublish

Résumé

Antimicrobial peptides (AMPs) preferentially permeate prokaryotic membranes via electrostatic binding and membrane remodeling. Such action is drastically suppressed by high salt due to increased electrostatic screening, thus it is puzzling how marine AMPs can possibly work. We examine as a model system, piscidin-1, a histidine-rich marine AMP, and show that ion-histidine interactions play unanticipated roles in membrane remodeling at high salt: Histidines can simultaneously hydrogen-bond to a phosphate and coordinate with an alkali metal ion to neutralize phosphate charge, thereby facilitating multidentate bonds to lipid headgroups in order to generate saddle-splay curvature, a prerequisite to pore formation. A comparison among Na

Identifiants

pubmed: 35352449
doi: 10.1002/anie.202108501
pmc: PMC9189074
mid: NIHMS1807189
doi:

Substances chimiques

Antimicrobial Peptides 0
Lipid Bilayers 0
Phosphates 0
Histidine 4QD397987E

Types de publication

Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

e202108501

Subventions

Organisme : NIH HHS
ID : T32GM008042
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008042
Pays : United States
Organisme : NIH HHS
ID : R01AI143730
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41GM103393
Pays : United States
Organisme : NIH HHS
ID : T32AR071307
Pays : United States
Organisme : NIH HHS
ID : T32GM008185
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM134047
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM067180
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM103393
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008185
Pays : United States
Organisme : NIAMS NIH HHS
ID : T32 AR071307
Pays : United States
Organisme : NIH HHS
ID : R01GM067180
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI143730
Pays : United States

Informations de copyright

© 2022 Wiley-VCH GmbH.

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Auteurs

Wujing Xian (W)

Department of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA.

Matthew R Hennefarth (MR)

Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.

Michelle W Lee (MW)

Department of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA.

Tran Do (T)

Department of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA.

Ernest Y Lee (EY)

Department of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA.

Anastassia N Alexandrova (AN)

Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
California Nano Systems Institute, University of California, Los Angeles, Los Angeles, CA 90095, USA.

Gerard C L Wong (GCL)

Department of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA.
California Nano Systems Institute, University of California, Los Angeles, Los Angeles, CA 90095, USA.

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