Structural Destabilization of Azurin by Imidazolium Chloride Ionic Liquids in Aqueous Solution

被引:17
作者
Acharyya, Arusha [1 ]
DiGiuseppi, David [2 ]
Stinger, Brittany L. [3 ]
Schweitzer-Stenner, Reinhard [2 ]
Vaden, Timothy D. [3 ]
机构
[1] Univ Penn, Dept Chem, 231 S 34 St, Philadelphia, PA 19104 USA
[2] Drexel Univ, Dept Chem, 32 S 32nd St, Philadelphia, PA 19104 USA
[3] Rowan Univ, Dept Chem & Biochem, 201 Mullica Hill Rd, Glassboro, NJ 08028 USA
关键词
BOVINE SERUM-ALBUMIN; AMIDE-I; MOLECULAR-DYNAMICS; FLUORESCENT PROTEIN; ENZYMATIC-ACTIVITY; REDOX-STATE; STABILITY; CONFORMATION; MYOGLOBIN; IMPACT;
D O I
10.1021/acs.jpcb.9b04113
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
Alkyl imidazolium chloride ionic liquids (ILs) have been used for numerous biochemical applications. Their hydrophobicity can be tuned by changing the alkyl chain length, and longer-chain ILs can form micelles in aqueous solution. We have investigated the effects of imidazolium chloride ILs on the structure and stability of azurin, which is a very stable Cu2+ redox protein with both alpha-helix and beta-sheet domains. Temperature-dependent infrared (IR) and vibrational circular dichroism spectroscopy can provide secondary-structure-specific information about how the protein is affected, and temperature-jump transient IR measurements can quantify the IL-influenced unfolding dynamics. Using these techniques, we can quantify how azurin is destabilized by 1.0 M ILs in aqueous solution. The shorter, less hydrophobic ILs, 1-butyl-3-methylimidazolium chloride and 1-hexyl-3-methylimidazolium chloride likely interact with the alpha-helix domain and decrease protein melting temperature from 82 degrees C without IL to SS degrees C and disturb the overall tertiary structure, resulting in a looser, more open shape. Thermodynamic analysis indicates that protein destabilization is due to increased unfolding entropy. 1-Octyl-3-methylimidazolium chloride [OMIM]Cl, which forms micelles in solution that may partially solvate the protein, has a more significant destabilizing effect, resulting in a melting temperature of 35 degrees C, larger unfolding entropy, and relaxation kinetics several orders of magnitude faster than with unperturbed azurin. The temperatureindependence of the relaxation time constant suggests that in the presence of [OMIM]Cl, the protein folding potential energy surface has become very smooth.
引用
收藏
页码:6933 / 6945
页数:13
相关论文
共 120 条
[1]   Synthesis, characterization, and liposome partition of a novel tetracycline derivative using the ionic liquids framework [J].
Alves, Filipa ;
Oliveira, Filipe S. ;
Schroeder, Bernd ;
Matos, Carla ;
Marrucho, Isabel M. .
JOURNAL OF PHARMACEUTICAL SCIENCES, 2013, 102 (05) :1504-1512
[2]   Elucidation of interactions of BSA with [EPMpyr]+[Cl]- using spectroscopic techniques with reference to theoretical thermodynamic and molecular docking studies [J].
Arumugam, Vasanthakumar ;
Rajamanikandan, Ramar ;
Ilanchelian, Malaichamy ;
Moodley, Kandasamy G. ;
Redhi, Gan G. .
JOURNAL OF MOLECULAR LIQUIDS, 2019, 273 :634-644
[3]   Thermodynamic characterization of the biocompatible ionic liquid effects on protein model compounds and their functional groups [J].
Attri, Pankaj ;
Venkatesu, Pannuru .
PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2011, 13 (14) :6566-6575
[4]   The infrared absorption of amino acid side chains [J].
Barth, A .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 2000, 74 (3-5) :141-173
[5]   Structure and Stability of Phospholipid Bilayers Hydrated by a Room-Temperature Ionic Liquid/Water Solution: A Neutron Reflectometry Study [J].
Benedetto, Antonio ;
Heinrich, Frank ;
Gonzalez, Miguel A. ;
Fragneto, Giovanna ;
Watkins, Erik ;
Ballone, Pietro .
JOURNAL OF PHYSICAL CHEMISTRY B, 2014, 118 (42) :12192-12206
[6]   Heme redox potentials hold the key to reactivity differences between nitric oxide reductase and heme-copper oxidase [J].
Bhagi-Damodaran, Ambika ;
Reed, Julian H. ;
Zhu, Qianhong ;
Shi, Yelu ;
Hosseinzadeh, Parisa ;
Sandoval, Braddock A. ;
Harnden, Kevin A. ;
Wang, Shuyan ;
Sponholtz, Madeline R. ;
Mirts, Evan N. ;
Dwaraknath, Sudharsan ;
Zhang, Yong ;
Moenne-Loccoz, Pierre ;
Lu, Yi .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2018, 115 (24) :6195-6200
[7]   Computational studies of room temperature ionic liquid-water mixtures [J].
Bhargava, B. L. ;
Yasaka, Yoshiro ;
Klein, Michael L. .
CHEMICAL COMMUNICATIONS, 2011, 47 (22) :6228-6241
[8]   Biamphiphilic Ionic Liquid Induced Folding Alterations in the Structure of Bovine Serum Albumin in Aqueous Medium [J].
Bharmoria, Pankaj ;
Rao, K. Srinivasa ;
Trivedi, Tushar J. ;
Kumar, Arvind .
JOURNAL OF PHYSICAL CHEMISTRY B, 2014, 118 (01) :115-124
[9]  
Bicout DJ, 2000, PROTEIN SCI, V9, P452
[10]   Protein engineering of cellulases [J].
Bommarius, Andreas S. ;
Sohn, Minjeong ;
Kang, Yuzhi ;
Lee, Jay H. ;
Realff, Matthew J. .
CURRENT OPINION IN BIOTECHNOLOGY, 2014, 29 :139-145