Nonionic amphiphilic polymers derived from Tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent.
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.
Prata
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Laboratoire de Physico-chimie Macromoléculaire, CNRS UMR 7615, ESPCI, 10 rue Vauquelin, F-75005 Paris, France.
Giusti
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F
Gohon
Y
Y
Pucci
B
B
Popot
J L
JL
Tribet
C
C
D000178:Acrylamides / Q000737:chemistry*; D001436:Bacteriorhodopsins / Q000737:chemistry / Q000187:drug effects; D003573:Cytochrome b Group / Q000737:chemistry / Q000187:drug effects; D045346:Cytochrome b6f Complex; D004355:Drug Stability; D008565:Membrane Proteins / Q000737:chemistry / Q000187:drug effects*; D011108:Polymers / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D011487:Protein Conformation / Q000187:drug effects; D012995:Solubility / Q000187:drug effects
D000178:Acrylamides; D003573:Cytochrome b Group; D008565:Membrane Proteins; D011108:Polymers; C445419:tris(hydroxymethyl)-acrylamidomethane; D001436:Bacteriorhodopsins; D045346:Cytochrome b6f Complex