Document Detail


Membrane channel formation by antimicrobial protegrins.
MedLine Citation:
PMID:  10446287     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Protegrins are small, arginine- and cysteine-rich, beta-sheet peptides with potent activity against bacteria, fungi, and certain enveloped viruses. We report that protegrins form weakly anion-selective channels in planar phospholipid bilayers, induce potassium leakage from liposomes and form moderately cation-selective channels in planar lipid membranes that contain bacterial lipopolysaccharide. The disruption of microbial membranes may be a central attribute related to the host defense properties of protegrins.
Authors:
Y Sokolov; T Mirzabekov; D W Martin; R I Lehrer; B L Kagan
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1420     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1999 Aug 
Date Detail:
Created Date:  1999-09-28     Completed Date:  1999-09-28     Revised Date:  2008-05-23    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  23-9     Citation Subset:  IM    
Affiliation:
Department of Psychiatry and Biobehavioral Sciences, UCLA Neuropsychiatric Institute, Suite 67-468 NPI, 750 Westwood Plaza, Los Angeles, CA 90024-1759, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Anti-Bacterial Agents / chemistry*,  pharmacology
Antimicrobial Cationic Peptides
Electrochemistry
Ion Channels / chemistry*,  drug effects
Lipid Bilayers / chemistry
Liposomes / chemistry
Molecular Sequence Data
Peptides / chemistry*,  pharmacology
Phospholipids / chemistry
Proteins / chemistry,  pharmacology
Grant Support
ID/Acronym/Agency:
AI 22839/AI/NIAID NIH HHS; AI 37945/AI/NIAID NIH HHS; MH 01174/MH/NIMH NIH HHS
Chemical
Reg. No./Substance:
0/Anti-Bacterial Agents; 0/Antimicrobial Cationic Peptides; 0/Ion Channels; 0/Lipid Bilayers; 0/Liposomes; 0/Peptides; 0/Phospholipids; 0/Proteins; 0/protegrin-1; 0/protegrin-3

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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