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Non-specific interactions between soluble proteins and lipids induce irreversible changes in the properties of lipid bilayers

TitleNon-specific interactions between soluble proteins and lipids induce irreversible changes in the properties of lipid bilayers
Publication TypeJournal Article
Year of Publication2013
AuthorsRuggeri F, Zhang F, Lind T, Bruce ED, Lau BLT, Cárdenas M
JournalSoft Matter
Volume9
Issue16
Start Page4219
Pagination4219-4226
Date Published03/2013
Abstract

Soluble  proteins  in the extracellular matrix experience a crowded environment. However, most of the biophysical studies performed to date have focused on  protein  concentrations within the dilute regime (well below the mM range). Here, we systematically studied the interaction of model cell membrane systems (giant unilamellar vesicles and supported  lipid  bilayers) with soluble globular  proteins , bovine serum albumin,  hemoglobin  and lysozyme at physiologically relevant concentrations. To mimic the extracellular environment more closely, we also used fetal bovine serum as a good representative of a biomimetic  protein  mixture. We found that regardless of the  protein  used (and thus of their biological function), the interactions between a model cell membrane and these  proteins  are determined by their physico-chemical characteristics, mainly their dipolar character (or charged patches). In this paper we discuss the specificity and reversibility of these interactions and their potential implications on the living cells. In particular, we report initial evidence for an additional role of  glycolipids  in cell membranes: that of reducing the effects of non-specific  adsorption  of soluble  proteins  on the cell membrane.

DOI10.1039/C3SM27769K