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Deceleration of Arginine Kinase Refolding by Induced Helical Structures

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Abstract

Arginine kinase (AK) is a key metabolic enzyme for keeping energy balance in invertebrates. Therefore, regulation of the enzymatic activity and the folding studies of AK from the various invertebrates have been the focus of investigation. We studied the effects of helical structures by using hexafluoroisopropanol (HFIP) on AK folding. Folding kinetic studies showed that the folding rates of the urea-denatured AKs were significantly decelerated after being induced in various concentrations of HFIP. AK lost its activity completely at concentrations greater than 60%. The results indicated that the HFIP-induced helical structures in the denatured state play a negative role in protein folding, and the helical structures induced in 5% (v/v) HFIP act as the most effective barrier against AK taking its native structure. The computational docking simulations (binding energies for −2.19 kcal/mol for AutoDock4.2 and −20.47 kcal/mol for Dock6.3) suggested that HFIP interacts with the several important residues that are predicted by both programs. The excessively pre-organized helical structures not only hampered the folding process, but also ultimately brought about changes in the three-dimensional conformation and biological function of AK.

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Abbreviations

AK:

Arginine kinase

HFIP:

1,1,1,3,3,3-Hexafluoroisopropanol

TFE:

2,2,2-Trifluoroethanol

CK:

Creatine kinase

ANS:

8-Anilino-1-naphthalenesulfonic acid

CD:

Circular dichroism

UV:

Ultraviolet

SDS:

Sodium dodecyl sulfate

PAGE:

Polyacrylamide gel electrophoresis

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Acknowledgments

This study was supported by the grants from the Science and Technology Bureau of Jiaxing, Zhejiang (No. 2008AY2032) and the Science and Technology Planning Project of Zhejiang Province (No. 2010C33139). Dr. Wei-Jiang Hu was supported by a grant from China Postdoctoral Science Foundation (No. 20060400467). Dr. Hae Young Chung was supported by National Research Foundation of Korea (NRF) grant funded by the Korea government (MOST) (No. 20090083538) and thanks Aging Tissue Bank for providing research information. Dr. Jun-Mo Yang was supported by the grant of the Korea Health 21 R&D Project (Ministry of Health, Welfare and Family Affairs, Republic of Korea, 01-PJ3-PG6-01GN12-0001) and by a grant (Grant No. C-A9-220-1) from Samsung Biomedical Research Institute.

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Authors and Affiliations

  1. Zhejiang Provincial Key Laboratory of Applied Enzymology, Yangtze Delta Region Institute of Tsinghua University, Jiaxing, 314006, People’s Republic of China

    Hai-Long Li, Fan-Guo Meng & Wei-Jiang Hu

  2. College of Biology and Chemical Engineering, Jiaxing University, Jiaxing, 314000, People’s Republic of China

    Sheng-Mei Zhou

  3. Molecular Inflammation Research Center for Aging Intervention (MRCA), College of Pharmacy, Pusan National University, Busan, 609-735, Korea

    Daeui Park, Hyoung Oh Jeong & Hae Young Chung

  4. Department of Dermatology, Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul, 135-710, Korea

    Jun-Mo Yang

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  1. Hai-Long Li
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Correspondence to Fan-Guo Meng or Wei-Jiang Hu.

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Li, HL., Zhou, SM., Park, D. et al. Deceleration of Arginine Kinase Refolding by Induced Helical Structures. Protein J 31, 267–274 (2012). https://doi.org/10.1007/s10930-012-9397-6

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