Browse > Article

CoMFA Analysis on Inhibitory Effect of $3{\beta}$-Hydroxy-12-oleanen-28-oic Acid Analogues on PTP-1B Activity and Prediction of Active Compounds  

Kim, Sang-Jin (Department of Cosmetic Science, Daejeon Health Sciences College)
Kim, Se-Gon (Division of Applied Biology and Chemistry, College of Agriculture and Life Science, Chungnam National University)
Sung, Nack-Do (Division of Applied Biology and Chemistry, College of Agriculture and Life Science, Chungnam National University)
Publication Information
Journal of the Society of Cosmetic Scientists of Korea / v.34, no.2, 2008 , pp. 109-115 More about this Journal
Abstract
The comparative molecular field analyses(CoMFA) models between the substituents with changing groups($R_1{\sim}R_4$) of $3{\beta}$-hydroxy-12-oleanen-28-oic acid derivatives as substrate molecule and their inhibitory activities($pI_{50}$) against protein tyrosine phosphatase(PTP)-1B were derived and discussed quantitatively. The optimized CoMFA F1 model have best predictability and fitness($r^2_{cv.}=0.654$ and $r^2_{ncv.}=0.995$). The order of contribution ratio (%) with CoMFA fields on the inhibitory activities was a steric field(53.0%), electrostatic field(36.2%) and hydrophobic field(10.8%). From the analytical results of CoMFA contour maps, the inhibitory activities were dependent on the R4 group in substrate molecules. Particularly, the new active compounds(P1 & P2) with the inhibitory activity against melanin synthesis were expected.
Keywords
oleanolic acid; protein tyrosine phosphatase(PTP) 1B; CoMFA; melanin; PLS;
Citations & Related Records
Times Cited By KSCI : 3  (Citation Analysis)
연도 인용수 순위
1 O. Ukkola and M. Santanielmi, Protein tyrosine phosphatase 1B: a new target for the treatment of obesity and associated co-morbidities, J. Intern. Med., 251, 467 (2002)   DOI   ScienceOn
2 G. Prota and R. H. Thompson, Melanin pigmentation in mammals, Endeavor., 35, 2 (1976)   DOI
3 N. D. Sung, T. Y. Yoon, J. H. Song, and H. S. Jung, Three dimensional quantitative structure-activity relationship on the fungicidal activites of new novel 2-alkoxyphenyl-3-phenylthioisoidoline-1-one derivative using the comparative molecular field analyses (CoMFA) methodology based on the different alignment approach, Korean Soc. Appl. Bio. Chem., 48, 82 (2005)   과학기술학회마을
4 C. K. Kim, K. A. Lee, H. Zhang, H. Cho, and B. S. Lee, Docking studies on formylchromone derivatives as protein tyrosine phosphatase 1B (PTP-1B) inhibitors, Bull. Korean Chem. Soc., 28, 1141 (2007)   DOI
5 G. E. Kellogg, S. F. Semus, and D. J. Abraham, HINT: A new method of empirical hydrophobic field calculation for CoMFA, J. Comput. Aid. Mol. Des., 5, 545 (1991)   DOI
6 J. S. Chen, C. Wei, and M. R. Marshall, Inhibition mechanism of kojic acid on polyphenol oxidase, J. Agric. Food Chem., 39, 1897 (1991)   DOI
7 R. D. Cramer, J. D. Bunce, and D. E. Patterson, Cross-validation, bootstrapping, and partial least squares compared with multiple regression in conventional QSAR studies, Quant. Struct. Act. Relat., 7, 18 (1988)   DOI
8 M. Akamatsu, Current state and perspectivies of 3D-QSAR, Curr. Topics Med. Chem., 2, 1381 (2002)   DOI   ScienceOn
9 Y. Ishihara, M. Oka, M. Tsunakawa, K. Tomota, M. Hatori, H. Yamamoto, H. Kamei, T. Miyaki, M. Konish, and T. Oki, Melanostatin, a new melanin synthesis inhibitor production, isolation, chemical properties, structure and biological activity, J. Antibiot., 44, 25 (1991)   DOI   PUBMED
10 A. B. Lerner and T. B. Fitzpatrick, Biochemistry of melanin formation, Physiol. Rev., 30, 19 (1950)
11 K. N. Tomita, N. Oda, M. Kamel, T. Miyaki, and T. Oki, A new screening method for melanin biosynthesis inhibitors using Streptomyces bikiniensis, J. Antibiotics, 12, 1601 (1990)
12 R. D. III. Cramer, D. E. Patterson, and J. E. Bunce, Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins, J. Am. Chem. Soc., 110, 5959 (1988)   DOI   ScienceOn
13 L. Wu and Z. Y. Zhan, Probing the function of the Asp128 in the lowe molecular weight protein tyrosine phosphatase catalyzed reaction A presteady state and steady state kinetic investigation, Biochemistry, 35, 5426 (1996)   DOI   ScienceOn
14 S. Takamatsu, M. C. Rho, M. Hayashi, K. Komiyama, H. Tanaka, and S. Omura, New inhibitiors of melanogenesis, OH-3984 K1 and K2, II, physico-chemical properties and structural elucidation, J. Antibiot., 46, 1526 (1993)   DOI   ScienceOn
15 R. Kerr, Parallel helix bundles and ion channels: molecular modeling via simulated annealing and restrained molecular dynamics, Biophys. J., 67, 1501 (1994)   DOI   ScienceOn
16 D. Lu, Agouti protein is an antagonist of the melanocyte stimulating hormone receptor, Nature, 371, 799 (1994)   DOI   ScienceOn
17 H. S. Raper, The anaerobic oxidases, Physiol. Rev., 8, 245 (1928)   DOI
18 H. Lihong, Drug discovery based on traditional Chinese medicine, Proceedings of international symposium on development of Chinese cosmetic technology, Soc. Cosmet. Scientists Korea, 31, 3 (2005)
19 S. W. Jung, D. S. Han, S. J. Kim, and M. J. Chun, Fementation of tyrosinase inhbitor in mushroom media, Kor. J. Appl. Microbiol. Biotechnol., 24, 227 (1996)
20 S. H. Lee, S. Y. Kim, J. J. Km, T. S. Jang, and S. R. Chung, The isolation of the inhbitory constituents on melanin polymer formation from the leaves of Cercis chinensis, Kor. J. Pharmacogn., 30(4), 397 (1999)   과학기술학회마을
21 L. Hu, J. Li, D. Hong, and Q. Ye, Triterpenes type protein tyrosine phosphatase 1B inhibitors and the preparation method and the use, China Patent, WO 2006/0609499 A1 (2006)
22 S. Akiu, Y. Suzuki, T. Asahara, Y. Fujinuma, and M. Fukuda, Inhibitory effect of arbutin on melanogenesis, Jpn. J. Dermatol., 101, 609 (1991)