Nonionic amphiphilic polymers derived from Tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent

C Prata; F Giusti; Y Gohon; B Pucci; J L Popot; C Tribet

doi:10.1002/1097-0282(2000)56:2<77::AID-BIP1053>3.0.CO;2-B

Nonionic amphiphilic polymers derived from Tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent

Biopolymers. 2000;56(2):77-84. doi: 10.1002/1097-0282(2000)56:2<77::AID-BIP1053>3.0.CO;2-B.

Authors

C Prata¹, F Giusti, Y Gohon, B Pucci, J L Popot, C Tribet

Affiliation

¹ Laboratoire de Physico-chimie Macromoléculaire, CNRS UMR 7615, ESPCI, 10 rue Vauquelin, F-75005 Paris, France.

PMID: 11592054
DOI: 10.1002/1097-0282(2000)56:2<77::AID-BIP1053>3.0.CO;2-B

Abstract

A new family of amphipols-amphiphilic polymers designed to form water-soluble complexes with membrane proteins-was synthesized by free-radical telomerization of Tris(hydroxymethyl)-acrylamidomethane (THAM) and derivatized THAM. Some of these polymers were found to prevent aggregation and denaturation of two model membrane proteins, bacteriorhodopsin and cytochrome b(6) f, in the absence of detergent micelles.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acrylamides / chemistry*
Bacteriorhodopsins / chemistry
Bacteriorhodopsins / drug effects
Cytochrome b Group / chemistry
Cytochrome b Group / drug effects
Cytochrome b6f Complex
Drug Stability
Membrane Proteins / chemistry
Membrane Proteins / drug effects*
Polymers / chemical synthesis*
Polymers / chemistry
Polymers / pharmacology*
Protein Conformation / drug effects
Solubility / drug effects

Substances

Acrylamides
Cytochrome b Group
Membrane Proteins
Polymers
tris(hydroxymethyl)-acrylamidomethane
Bacteriorhodopsins
Cytochrome b6f Complex