Document Detail


Binding of Cell-penetrating Penetratin Peptides to Plasma Membrane Vesicles Correlates Directly with Cellular Uptake.
MedLine Citation:
PMID:  21447320     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Cell-penetrating peptides (CPPs) gain access to intracellular compartments mainly via endocytosis and have capacity to deliver macromolecular cargo into cells. Although the involvement of various endocytic routes has been described it is still unclear what interactions are involved in eliciting an uptake response and to what extent affinity for particular cell surface components may determine the efficiency of a particular CPP. Previous biophysical studies of the interaction between CPPs and either lipid vesicles or soluble sugar-mimics of cell surface proteoglycans, the two most commonly suggested CPP binding targets, have not allowed quantitative correlationsto be established. We here explore the use of plasma membrane vesicles (PMVs) derived from cultured cells as cell surface models in biophysical experiments. Further, we examine the relationship between affinity to PMVs and uptake into live cells using the CPP penetratin and two mutants enriched in arginines and lysines respectively. We show, using centrifugation to sedimentPMVs, that the amount of peptide in the pellet fraction correlates linearly with the degree of cell internalization and that the relative efficiency of all-arginine and all-lysine variants of penetratin can be ascribed to their respective cell surface affinities. Our data showdifferences between arginine- and lysine-rich variants of penetratinthat has not been previously accounted for in studies using lipid vesicles. Our data also indicate greater differences in binding affinity to PMVs than to heparin, a commonly used cell surface proteoglycan mimic. Taken together, this suggests that the cell surface interactions of CPPsare dependent on several cell surface moieties and their molecular organization on the plasma membrane.
Authors:
Helene L Amand; Carolina L Boström; Per Lincoln; Bengt Nordén; Elin K Esbjörner
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-3-26
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  -     ISSN:  0006-3002     ISO Abbreviation:  -     Publication Date:  2011 Mar 
Date Detail:
Created Date:  2011-3-30     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2010. Published by Elsevier B.V.
Affiliation:
Department of Chemical and Biological Engineering/Physical Chemistry, Chalmers University of Technology, Kemivägen 10, S-412 96 Gothenburg, Sweden.
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