The Role of Decorated SDS Micelles in Sub-CMC Protein Denaturation and Association

被引:136
作者
Andersen, Kell K. [1 ,2 ]
Oliveira, Cristiano L. [3 ,4 ]
Larsen, Kim L. [2 ]
Poulsen, Flemming M. [5 ]
Callisen, Thomas H. [6 ]
Westh, Peter [7 ]
Pedersen, Jan S. [7 ]
Otzen, Daniel [1 ]
机构
[1] Univ Aarhus, Interdisciplinary Nanosci Ctr, DK-8000 Aarhus C, Denmark
[2] Aalborg Univ, Dept Life Sci, DK-9000 Aalborg, Denmark
[3] Univ Aarhus, Dept Chem, iNANO Interdisciplinary Nanosci Ctr, DK-8000 Aarhus C, Denmark
[4] Univ Aarhus, Ctr mRNP Biogenesis & Metab, DK-8000 Aarhus C, Denmark
[5] Univ Copenhagen, Dept Mol Biol, Struct Biol & NMR Lab, DK-2200 Copenhagen, Denmark
[6] Novozymes AS, DK-2880 Bagsvaerd, Denmark
[7] Roskilde Univ, NSM Funct Biomat, DK-4000 Roskilde, Denmark
关键词
ACBP; surfactant; isothermal titration calorimetry; small-angle X-ray scattering; dimerization; SODIUM-DODECYL-SULFATE; HUMICOLA-INSOLENS CUTINASE; RAY SOLUTION SCATTERING; SURFACTANT INTERACTIONS; BIOLOGICAL MACROMOLECULES; KINETIC STABILITY; FIBRIL FORMATION; ACYL-COENZYME; BINDING; LYSOZYME;
D O I
10.1016/j.jmb.2009.06.019
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
We have combined spectroscopy, chromatography, calorimetry, and small-angle X-ray scattering (SAXS) to provide a comprehensive structural and stoichiometric description of the sodium dodecyl sulfate (SDS)-induced denaturation of the 86-residue alpha-helical bovine acyl-coenzyme-A-binding protein (ACBP). Denaturation is a multistep process. Initial weak binding of 1-3 SDS molecules per protein molecule below 1.3 m_M does not perturb the tertiary structure. Subsequent binding of similar to 13 SDS molecules per ACBP molecule leads to the formation of SDS aggregates on the protein and changes in both tertiary and secondary structures. SAXS data show that, at this stage, a decorated micelle links two ACBP molecules together, leaving about half of the polypeptide chain as a disordered region protruding into the solvent. Further titration with SDS leads to the additional uptake of 26 SDS molecules, which, according to SAXS, forms a larger decorated micelle bound to a single ACBP molecule. At the critical micelle concentration, we conclude from reduced mobility and increased fluorescence anisotropy that each ACBP molecule becomes associated with more than one micelle. At this point, 56-60 SDS molecules are bound per ACBP molecule. Our data provide key structural insights into decorated micelle complexes with proteins, revealing a remarkable diversity in the different conformations they can stabilize. The data highlight that a minimum decorated micelle size, which may be a key driving force for intermolecular protein association, exists. This may also provide a structural basis for the known ability of submicellar surfactant concentrations to induce protein aggregation and fibrillation. (c) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码:207 / 226
页数:20
相关论文
共 67 条
[1]   Global study of myoglobin-surfactant interactions [J].
Andersen, Kell K. ;
Westh, Peter ;
Otzen, Daniel E. .
LANGMUIR, 2008, 24 (02) :399-407
[2]   Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system [J].
Bagger, Heidi L. ;
Hoffmann, Soren V. ;
Fuglsang, Claus C. ;
Westh, Peter .
BIOPHYSICAL CHEMISTRY, 2007, 129 (2-3) :251-258
[3]   Reconstruction of protein form with X-ray solution scattering and a genetic algorithm [J].
Chacón, P ;
Díaz, JF ;
Morán, F ;
Andreu, JM .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 299 (05) :1289-1302
[4]   Low-resolution structures of proteins in solution retrieved from X-ray scattering with a genetic algorithm [J].
Chacón, P ;
Morán, F ;
Díaz, JF ;
Pantos, E ;
Andreu, JM .
BIOPHYSICAL JOURNAL, 1998, 74 (06) :2760-2775
[5]   Studies on surfactant-biopolymer interaction. I. Microcalorimetric investigation on the interaction of cetyltrimethylammonium bromide (CTAB) and sodium dodecylsulfate (SDS) with gelatin (Gn), lysozyme (Lz) and deoxyribonucleic acid (DNA) [J].
Chatterjee, A ;
Moulik, SP ;
Majhi, R ;
Sanyal, SK .
BIOPHYSICAL CHEMISTRY, 2002, 98 (03) :313-327
[6]   Kinetic stability as a mechanism for protease longevity [J].
Cunningham, EL ;
Jaswal, SS ;
Sohl, JL ;
Agard, DA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (20) :11008-11014
[7]   Fluorescence probing of albumin-surfactant interaction [J].
De, S ;
Girigoswami, A ;
Das, S .
JOURNAL OF COLLOID AND INTERFACE SCIENCE, 2005, 285 (02) :562-573
[8]   COLLAGEN FIBRIL FORMATION IN THE PRESENCE OF SODIUM DODECYL-SULFATE [J].
DOMBI, GW ;
HALSALL, HB .
BIOCHEMICAL JOURNAL, 1985, 228 (03) :551-556
[9]   SOLUBILIZATION OF DRUGS IN MICELLAR SYSTEMS STUDIED BY ELUENT GEL-PERMEATION CHROMATOGRAPHY [J].
DRAPER, M ;
SAVAGE, M ;
COLLETT, JH ;
ATTWOOD, D ;
PRICE, C ;
BOOTH, C ;
WANG, QG .
PHARMACEUTICAL RESEARCH, 1995, 12 (08) :1231-1237
[10]   Peracetylated bovine carbonic anhydrase (BCA-Ac18) is kinetically more stable than native BCA to sodium dodecyl sulfate [J].
Gitlin, I ;
Gudiksen, KL ;
Whitesides, GM .
JOURNAL OF PHYSICAL CHEMISTRY B, 2006, 110 (05) :2372-2377