Physical-chemical features of non-detergent sulfobetaines active as protein-folding helpers

被引:39
作者
Expert-Bezançon, N
Rabilloud, T
Vuillard, L
Goldberg, ME [1 ]
机构
[1] Inst Pasteur, Unite Repliement & Modelisat Prot, Paris, France
[2] CEA, DBMS, BECP, Grenoble, France
[3] Inst Laue Langevin, Grenoble, France
关键词
physical-chemical features; non-detergent sulfobetaines; protein-folding helpers;
D O I
10.1016/S0301-4622(02)00299-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Some non-detergent sulfobetaines had been shown to prevent aggregation and improve the yield of active proteins when added to the buffer during in vitro protein renaturation. With the aim of designing more efficient folding helpers, a series of non-detergent sulfobetaines have been synthesized and their efficiency in improving the renaturation of a variety of proteins (E. coli tryptophan synthase and beta-D-galactosidase, hen lysozyme, bovine serum albumin, a monoclonal antibody) have been investigated. Attempts to correlate the structure of each sulfobetaines with its effect on folding revealed some molecular features that appear important in helping renaturation. This enabled us to design and synthesize new non-detergent sulfobetaines that act as potent folding helpers. (C) 2002 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:469 / 479
页数:11
相关论文
共 21 条
[1]   REFOLDING HUMAN-SERUM ALBUMIN AT RELATIVELY HIGH PROTEIN-CONCENTRATION [J].
BURTON, SJ ;
QUIRK, AV ;
WOOD, PC .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1989, 179 (02) :379-387
[2]   Preparation of functional recombinant protein from E-coli using a nondetergent sulfobetaine [J].
Chong, YC ;
Chen, HW .
BIOTECHNIQUES, 2000, 29 (06) :1166-1167
[3]   Functions of the subunits in the FlhD2C2 transcriptional master regulator of bacterial flagellum biogenesis and swarming [J].
Claret, L ;
Hughes, C .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 303 (04) :467-478
[4]   STRUCTURAL AND FUNCTIONAL INFLUENCE OF ENZYME ANTIBODY INTERACTIONS - EFFECTS OF 8 DIFFERENT MONOCLONAL-ANTIBODIES ON THE ENZYMATIC-ACTIVITY OF ESCHERICHIA-COLI TRYPTOPHAN SYNTHASE [J].
DJAVADIOHANIANCE, L ;
FRIGUET, B ;
GOLDBERG, ME .
BIOCHEMISTRY, 1984, 23 (01) :97-104
[5]   KINETIC STUDIES OF TRYPTOPHAN SYNTHETASE - INTERACTION OF SUBSTRATES WITH B SUBUNIT [J].
FAEDER, EJ ;
HAMMES, GG .
BIOCHEMISTRY, 1970, 9 (21) :4043-&
[6]   POLYPEPTIDE-ANTIBODY BINDING MECHANISM - CONFORMATIONAL ADAPTATION INVESTIGATED BY EQUILIBRIUM AND KINETIC-ANALYSIS [J].
FRIGUET, B ;
DJAVADIOHANIANCE, L ;
GOLDBERG, ME .
RESEARCH IN IMMUNOLOGY, 1989, 140 (04) :355-376
[7]  
Friguet B., 1997, PROTEIN STRUCTURE PR, P323
[8]   Non-detergent sulphobetaines: A new class of molecules that facilitate in vitro protein renaturation [J].
Goldberg, ME ;
ExpertBezancon, N ;
Vuillard, L ;
Rabilloud, T .
FOLDING & DESIGN, 1996, 1 (01) :21-27
[9]   A KINETIC-STUDY OF THE COMPETITION BETWEEN RENATURATION AND AGGREGATION DURING THE REFOLDING OF DENATURED REDUCED EGG-WHITE LYSOZYME [J].
GOLDBERG, ME ;
RUDOLPH, R ;
JAENICKE, R .
BIOCHEMISTRY, 1991, 30 (11) :2790-2797
[10]   REFOLDING AND REACTIVATION OF ESCHERICHIA-COLI TRYPTOPHAN SYNTHASE BETA-2 SUBUNIT AFTER INACTIVATION AND DISSOCIATION IN GUANIDINE-HYDROCHLORIDE AT ACIDIC PH [J].
GROHA, C ;
BARTHOLMES, P ;
JAENICKE, R .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1978, 92 (02) :437-441