Thermodynamic studies and binding mechanisms of cell-penetrating peptides with lipids and glycosaminoglycans.

Abstract:

:Cell-penetrating peptides (CPPs) traverse the membrane of biological cells at low micromolar concentrations and are able to take various cargo molecules along with. Despite large differences in their chemical structure, CPPs share the structural similarity of a high cationic charge density. This property confers to them the ability to bind electrostatically membrane constituents such as anionic lipids and glycosaminoglycans (GAGs). Controversies exist, however, about the biological response after the interaction of CPPs with such membrane constituents. Present review compares thermodynamic binding studies with conditions of the biological CPP uptake. It becomes evident that CPPs enter biological cells by different and probably competing mechanisms. For example, some amphipathic CPPs traverse pure lipid model membranes at low micromolar concentrations--at least in the absence of cargos. In contrast, no direct translocation at these conditions is observed for non-amphipathic CPPs. Finally, CPPs bind GAGs at low micromolar concentrations with potential consequences for endocytotic pathways.

journal_name

Adv Drug Deliv Rev

authors

Ziegler A

doi

10.1016/j.addr.2007.10.005

subject

Has Abstract

pub_date

2008-03-01 00:00:00

pages

580-97

issue

4-5

eissn

0169-409X

issn

1872-8294

pii

S0169-409X(07)00292-X

journal_volume

60

pub_type

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