Document Detail


Impact of peptide clustering on unbinding forces in the context of fusion mimetics.
MedLine Citation:
PMID:  23261469     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Coiled-coil zipping and unzipping is a pivotal process in SNARE regulated membrane fusion. In this study we examine this process mediated by a minimal model for coiled-coil formation employing force spectroscopy in the context of membrane-coated surfaces and probes. The interaction forces are the range of several hundredpN surprisingly low considering the proposed amount of molecular bonds in the contact zone. However, by means of high-resolution imaging employing atomic force microscopy and studying the lateral mobility of lipids and peptides as a function of coiled-coil formation, we are able to supply a detailed view on processes occurring on the membrane surfaces during force measurements. The interaction forces determined here are not only dependent on the peptide concentration on the surface, but also on the regional organization of lateral peptide clusters found prior to coiled-coil formation.
Authors:
Gesa Pähler; Bärbel Lorenz; Andreas Janshoff
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-12-19
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  -     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-25     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012. Published by Elsevier Inc.
Affiliation:
Institute of Physical Chemistry, Tammannstr. 6, Georg-August-University Göttingen, 37077 Göttingen, Germany.
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