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Binding of cell-penetrating penetratin peptides to plasma membrane vesicles correlates directly with cellular uptake

Helene Åmand (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; Carolina Boström (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; Per Lincoln (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; Bengt Nordén (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; E. K. Esbjorner
Biochimica Et Biophysica Acta-Biomembranes (0005-2736). Vol. 1808 (2011), 7, p. 1860-1867.
[Artikel, refereegranskad vetenskaplig]

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 which 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 correlations to be established. We here explore the use of plasma membrane vesicles (PMVs) derived from cultured mammalian cells as cell surface models in biophysical experiments. Further, we examine the relationship between affinity for PMVs and uptake into live cells using the CPP penetratin and two analogs enriched in arginines and lysines respectively. We show, using centrifugation to sediment PMVs, 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 show differences between arginine- and lysine-rich variants of penetratin that 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 CPPs are dependent on several cell surface moieties and their molecular organization on the plasma membrane. (C) 2011 Elsevier BM. All rights reserved.

Nyckelord: Cell-penetrating peptide, Penetratin, Plasma membrane vesicles, Membrane affinity, Arginine, Lysine, human immunodeficiency virus, arginine-rich peptides, heparan-sulfate, lipid-membranes, bilayer-membranes, enters cells, tat peptide, translocation, endocytosis, macropinocytosis



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Denna post skapades 2011-06-30.
CPL Pubid: 142717

 

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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Fysikalisk kemi (2005-2014)

Ämnesområden

Energi
Livsvetenskaper
Materialvetenskap
Nanovetenskap och nanoteknik
Biokemi

Chalmers infrastruktur

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