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Chem Soc Rev. 2012 Mar 7;41(5):1721-8. doi: 10.1039/c1cs15180k. Epub 2011 Nov 15.

Designer peptide surfactants stabilize diverse functional membrane proteins.

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1
Center for Biomedical Engineering, Massachusetts Institute of Technology, NE47, 500 Technology Square, Cambridge, MA 02139-4307, USA. sotiris@mit.edu

Abstract

Multi-spanning integral membrane proteins, including G-protein coupled receptors (GPCR), ion channels, and ion transporters, comprise a major class of drug targets. However, despite their vital importance, most molecular structures of membrane proteins remain elusive. This is largely due to lack of effective materials and methods to stabilize their functional conformation for sufficient time. Thus finding optimal surfactants and developing new approaches to study fundamental properties of unstable membrane proteins is urgently needed. In this tutorial review we summarize designer peptides with surfactant properties and their usefulness to stabilize membrane proteins. These peptide surfactants present new opportunities for the stabilization and characterization of diverse membrane proteins. Previous studies on the interaction between surfactant peptides and membrane proteins revealed strategies to design new peptides tailor-made for the stabilization of specific proteins. We review examples of solubilization, purification, long-term stabilization of membrane proteins, and the design principles of peptide sequences. We discuss future trends for exploiting spatial features, thermodynamic parameters, and self-assembling properties to create peptide surfactant structures to facilitate the characterization of diverse membrane proteins.

PMID:
22086544
DOI:
10.1039/c1cs15180k
[Indexed for MEDLINE]
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