Mechanical Insight into Resistance of Betaine to Urea-Induced Protein Denaturation

被引：12

作者：

Chen, Jiantao ^{[1
]}

Gong, Xiangjun ^{[1
]}

Zeng, Chaoxi ^{[2
]}

Wang, Yonghua ^{[2
]}

Zhang, Guangzhao ^{[1
]}

机构：

[1] South China Univ Technol, Fac Mat Sci & Engn, Guangzhou 510640, Guangdong, Peoples R China

[2] South China Univ Technol, Coll Light Ind & Food Sci, Guangzhou 510640, Guangdong, Peoples R China

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2016年 / 120卷 / 48期

基金：

中国国家自然科学基金;

关键词：

NUCLEAR-MAGNETIC-RESONANCE; MOLECULAR-DYNAMICS SIMULATION; TRIMETHYLAMINE N-OXIDE; GLYCINE BETAINE; GUANIDINE-HYDROCHLORIDE; AQUEOUS-SOLUTIONS; ALPHA-CHYMOTRYPSIN; STRUCTURE BREAKER; WATER; BEHAVIOR;

D O I：

10.1021/acs.jpcb.6b10172

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

It is known that urea can induce protein denaturation that can be inhibited by osmolytes. Yet, experimental explorations on this mechanism at the molecular level are still lacking. We have investigated the resistance of betaine to the urea-induced denaturation of lysozyme in aqueous solutions using low-field NMR. Our study demonstrates that urea molecules directly interact with lysozyme, leading to denaturation. However, betaine molecules interacting with urea more strongly than lysozyme can pull the bound urea molecules from lysozyme so that the protein is protected from denaturation. The number of urea molecules bound to a betaine molecule is given under different conditions. Proton NMR spectroscopy (H-1-NMR) and Fourier transform infrared spectroscopy reveal that the interaction between betaine and urea is through hydrogen bonding.

引用

页码：12327 / 12333

页数：7

共 49 条

[1]

Anna K., 2010, CHEM PHYS, V133

[2] Molecular Dynamics Simulation of Aqueous Urea Solution: Is Urea a Structure Breaker? [J].

Bandyopadhyay, Dibyendu ;

Mohan, Sadhana ;

Ghosh, Swapan K. ;

Choudhury, Niharendu .

JOURNAL OF PHYSICAL CHEMISTRY B, 2014, 118 (40) :11757-11768

[3] Counteraction of urea-induced protein denaturation by trimethylamine N-oxide:: A chemical chaperone at atomic resolution [J].

Bennion, BJ ;

Daggett, V .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (17) :6433-6438

[4] Effect of Urea on the β-Hairpin Conformational Ensemble and Protein Denaturation Mechanism [J].

Berteotti, Anna ;

Barducci, Alessandro ;

Parrinello, Michele .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2011, 133 (43) :17200-17206

[5] RELAXATION EFFECTS IN NUCLEAR MAGNETIC RESONANCE ABSORPTION [J].

BLOEMBERGEN, N ;

PURCELL, EM ;

POUND, RV .

PHYSICAL REVIEW, 1948, 73 (07) :679-712

[6] EFFECTS OF DIFFUSION ON FREE PRECESSION IN NUCLEAR MAGNETIC RESONANCE EXPERIMENTS [J].

CARR, HY ;

PURCELL, EM .

PHYSICAL REVIEW, 1954, 94 (03) :630-638

[7] Molecular dynamics simulation of aqueous solutions of glycine betaine [J].

Civera, M ;

Fornili, A ;

Sironi, M ;

Fornili, SL .

CHEMICAL PHYSICS LETTERS, 2003, 367 (1-2) :238-244

[8] The use of solvent relaxation NMR to study colloidal suspensions [J].

Cooper, Catherine L. ;

Cosgrove, Terence ;

van Duijneveldt, Jeroen S. ;

Murray, Martin ;

Prescott, Stuart W. .

SOFT MATTER, 2013, 9 (30) :7211-7228

[9] Effect of urea on biomimetic systems: Neither water 3-D structure rupture nor direct mechanism, simply a more "polar water" [J].

Dias, LG ;

Florenzano, FH ;

Reed, WF ;

Baptista, MS ;

Souza, SMB ;

Alvarez, EB ;

Chaimovich, H ;

Cuccovia, IM ;

Amaral, CLC ;

Brasil, CR ;

Romsted, LS ;

Politi, MJ .

LANGMUIR, 2002, 18 (02) :319-324

[10] Quantifying Additive Interactions of the Osmolyte Proline with Individual Functional Groups of Proteins: Comparisons with Urea and Glycine Betaine, Interpretation of m-Values [J].

Diehl, Roger C. ;

Guinn, Emily J. ;

Capp, Michael W. ;

Tsodikov, Oleg V. ;

Record, M. Thomas, Jr. .

BIOCHEMISTRY, 2013, 52 (35) :5997-6010

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