The influence of flavonoid compounds on the in vitro inhibition study of a human fibroblast collagenase catalytic domain expressed in E. coli

Enzyme and Microbial Technology

Volumn 52, Issue 1, 2013, Pages 26-31

  Nguyen, Thi Thanh Hanh ^a   Moon, Young Hwan ^b   Ryu, Young Bae ^c   Kim, Young Min ^c   Nam, Seung Hee ^d   Kim, Mi Sook ^e   Kimura, Atsuo ^f   Kim, Doman ^a  

^a Chonnam National University   (South Korea)

^b Audubon Sugar Institute   (United States)

^c Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^d Jeonnam Agricultural Research and Extension Service   (South Korea)

^e Dankook University   (South Korea)

^f HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Catechin; Epigallocatechin gallate; Expression; Inhibition; Matrix metalloproteinase MMP 1; Molecular docking

Indexed keywords

CATECHIN; EPIGALLOCATECHIN GALLATE; EXPRESSION; MATRIX METALLOPROTEINASES; MOLECULAR DOCKING;

BINDING ENERGY; CELL CULTURE; ENZYME ACTIVITY; ENZYME INHIBITION; ESCHERICHIA COLI; FIBROBLASTS; FLAVONOIDS; HYDROGEN BONDS; PHENOLS;

COMPLEXATION;

ALANINE; AMPELOPSIN; ARGININE; COLLAGEN FIBRIL; DAIDZEIN; EPICATECHIN; EPICATECHIN GALLATE; EPIGALLOCATECHIN; EPIGALLOCATECHIN GALLATE; FLAVONOID; GALLIC ACID; GALLOCATECHIN GALLATE; INTERSTITIAL COLLAGENASE; LEUCINE; PROLINE; PUERARIN; QUERCETIN; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DRUG STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; FIBROBLAST; HUMAN; HUMAN FIBROBLAST COLLAGENASE CATALYTIC DOMAIN GENE; HYDROGEN BOND; HYDROPHOBICITY; IC 50; IN VITRO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN EXPRESSION; RECOMBINANT GENE;

BINDING, COMPETITIVE; CATALYSIS; CATALYTIC DOMAIN; CATECHIN; COLLAGENASES; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; FIBROBLASTS; FLAVONOIDS; GALLIC ACID; HUMANS; HYDROGEN BONDING; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; INHIBITORY CONCENTRATION 50; MATRIX METALLOPROTEINASE 1; MATRIX METALLOPROTEINASE INHIBITORS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 84870368722     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2012.10.001     Document Type: Article

References (27)

1. Nagase H., Woessner J.F. Matrix metalloproteinases. Journal of Biological Chemistry 1999, 274:21491-21494.
2. Vu T.H., Werb Z. Matrix metalloproteinases: effectors of development and normal physiology. Genes and Development 2000, 14:2123-2133.
3. Visse R., Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases-structure, function, and biochemistry. Circulation Research 2003, 92:827-839.
4. Iyer S., Wei S., Brew K., Acharya K.R. Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1. Journal of Biological Chemistry 2007, 282:364-371.
5. Aimes R.T., Quigley J.P. Matrix metalloproteinase-2 is an interstitial collagenase-inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type-I collagen generating the specific 3/4-length and 1/4-length fragments. Journal of Biological Chemistry 1995, 270:5872-5876.
6. Ohuchi E., Imai K., Fujii Y., Sato H., Seiki M., Okada Y. Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. Journal of Biological Chemistry 1997, 272:2446-2451.
7. Liu A.L., Wang H.D., Lee S.M.Y., Wang Y.T., Du G.H. Structure-activity relationship of flavonoids as influenza virus neuraminidase inhibitors and their in vitro anti-viral activities. Bioorganic and Medicinal Chemistry 2008, 16:7141-7147.
8. Teillet F., Boumendjel A., Boutonnat J., Ronot X. Flavonoids as RTK inhibitors and potential anticancer agents. Medicinal Research Reviews 2008, 28:715-745.
9. de Groot H., Rauen U. Tissue injury by reactive oxygen species and the protective effects of flavonoids. Fundamental and Clinical Pharmacology 1998, 12:249-255.
10. Middleton E., Kandaswami C. Effects of flavonoids on immune and inflammatory cell functions. Biochemical Pharmacology 1992, 43:1167-1179.
11. Tadera K., Minami Y., Takamatsu K., Matsuoka T. Inhibition of alpha-glucosidase and alpha-amylase by flavonoids. Journal of Nutritional Science and Vitaminology 2006, 52:149-153.
12. Kamiyama O., Sanae F., Ikeda K., Higashi Y., Minami Y., Asano N., et al. In vitro inhibition of alpha-glucosidases and glycogen phosphorylase by catechin gallates in green tea. Food Chemistry 2010, 122:1061-1066.
13. Zaveri N.T. Green tea and its polyphenolic catechins: medicinal uses in cancer and noncancer applications. Life Sciences 2006, 78:2073-2080.
14. Khan N., Afaq F., Saleem M., Ahmad N., Mukhtar H. Targeting multiple signaling pathways by green tea polyphenol (-)-epigallocatechin-3-gallate. Cancer Research 2006, 66:2500-2505.
15. Higdon J.V., Frei B. Tea catechins and polyphenols: health effects, metabolism, and antioxidant functions. Critical Reviews in Food Science and Nutrition 2003, 43:89-143.
16. Yang C.S., Wang X. Green tea and cancer prevention. Nutrition and Cancer 2010, 62:931-937.
17. Wolfram S., Wang Y., Thielecke F. Anti-obesity effects of green tea: from bedside to bench. Molecular Nutrition and Food Research 2006, 50:176-187.
18. Hamiltonmiller J.M.T. Antimicrobial properties of tea (Camellia-sinensis L). Antimicrobial Agents and Chemotherapy 1995, 39:2375-2377.
19. Shankar S., Ganapathy S., Hingorani S.R., Srivastava R.K. EGCG inhibits growth, invasion, angiogenesis and metastasis of pancreatic cancer. Frontiers in Bioscience 2008, 13:440-452.
20. Pirard B., Matter H. Matrix metalloproteinase target family landscape: a chemometrical approach to ligand selectivity based on protein binding site analysis. Journal of Medicinal Chemistry 2006, 49:51-69.
21. Pathak N., Hu S.I., Koehn J.A. The expression, refolding, and purification of the catalytic domain of human collagenase-3 (MMP-13). Protein Expression and Purification 1998, 14:283-288.
22. Parkar A.A., Stow M.D., Smith K., Panicker A.K., Guilloteau J.P., Jupp R., et al. Large-scale expression, refolding, and purification of the catalytic domain of human macrophage metalloelastase (MMP-12) in Escherichia coli. Protein Expression and Purification 2000, 20:152-161.
23. Morris G.M., Goodsell D.S., Halliday R.S., Huey R., Hart W.E., Belew R.K., et al. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. Journal of Computational Chemistry 1998, 19:1639-1662.
24. Nguyen T.T., Woo H.J., Kang H.K., Nguyen V.D., Kim Y.M., Kim D.W., et al. Flavonoid-mediated inhibition of SARS coronavirus 3C-like protease expressed in Pichia pastoris. Biotechnology Letters 2012, 34:831-838.
25. Borkakoti N., Winkler F.K., Williams D.H., D'Arcy A., Broadhurst M.J., Brown P.A., et al. Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor. Natural Structural Biology 1994, 1:106-110.
26. Nguyen T.T., Ryu H.J., Lee S.H., Hwang S., Breton V., Rhee J.H., et al. Virtual screening identification of novel severe acute respiratory syndrome 3C-like protease inhibitors and in vitro confirmation. Bioorganic and Medicinal Chemistry Letters 2011, 21:3088-3091.
27. Wallace A.C., Laskowski R.A., Thornton J.M. Ligplot-a program to generate schematic diagrams of protein ligand interactions. Protein Engineering 1995, 8:127-134.