Browse > Article
http://dx.doi.org/10.5012/bkcs.2008.29.5.959

Docking and Virtual Screening Studies for New Leads of Boar Salivary Lipocalin  

Sung, Nack-Do (Research Center for Transgenic Cloned Pigs, Division of Applied Biology & Chemistry, Chungnam National University)
Park, Chang-Sik (Research Center for Transgenic Cloned Pigs, Division of Applied Biology & Chemistry, Chungnam National University)
Park, Hyung-Yeon (Department of Chemistry, Inha University)
Kim, Chan-Kyung (Department of Chemistry, Inha University)
Publication Information
Bulletin of the Korean Chemical Society / v.29, no.5, 2008 , pp. 959-962 More about this Journal
Abstract
We have performed FlexX docking experiments to predict the best docking poses of 5-androst-16-en-3-ol or 5-androst-16-en-3-one to Boar salivary lipocalin (SAL). Since no steroids were found inside of the binding pocket of the X-ray structure of 1GM6, we tried to find docking structures after opening the pocket using the random tweak option implemented in SYBYL. This operation allowed the ligand to enter the pocket. The best poses generated from FlexX were different from the structures reported earlier, which calculated docking poses by manual docking followed by minimization. Analysis of docking poses allowed us to identify pharmacophores. From this information, virtual screening experiments using UNITY were performed. Among six candidates, 3-(3,7-dimethyloct-6-enylamino)propane-1,2-diol (Leadquest code name: 5755) was chosen for further development. Future work will involve synthesis of some derivatives of 5755 and biological experiments if any derivatives can control the biostimulation and improve reproductive efficiency in pigs.
Keywords
Boar salivary lipocalin; Steroid pheromones; FlexX docking; UNITY virtual screening
Citations & Related Records
Times Cited By KSCI : 3  (Citation Analysis)
Times Cited By Web Of Science : 0  (Related Records In Web of Science)
Times Cited By SCOPUS : 0
연도 인용수 순위
1 Clark, R. D. J. Chem. inf. Compt. Sci. 1997, 37, 1181   DOI   ScienceOn
2 Shenkin, P. S.; Yarmush, D. L.; Fine, R. M.; Wang, H.; Levinthal, C. Biopolymers 1987, 26, 2053   DOI   ScienceOn
3 Hoffmann, D.; Kramer, B.; Washio, T.; Steinmetzer, T.; Rarey, M.; Lengauer, T. J. Med. Chem. 1999, 42, 4422   DOI   ScienceOn
4 SYBYL 6.9; TRIPOS Inc.: St. Louis, USA
5 Powel, M. J. D. Mathematical Programming 1977, 12, 241   DOI
6 Clark, M.; Crammer, R. D.; Opdenbosch, N. V. J. Comput. Chem. 1989, 10, 982   DOI
7 Dixon, D. A.; Zeroka, D. J.; Wendoloski, J. J.; Wasserman, Z. R. J. Phys. Chem. 1985, 89, 5334   DOI
8 TOPKAT, version 6.2; Acclerys Inc.: San Diego, CA, 2001
9 Lead Quest Chemical Compound Libraries; Tripos, Inc.: St.Louis, MO, 2000; Vol. 1-3
10 Gower, D. B.; Booth, W. D. Ontog. Olfaction 1986, 255
11 Melrose, D. R.; Reed, H. C.; Patterson, R. L. Br. Veteri. J. 1971, 127, 497   DOI
12 Reed, H. C. B.; Melrose, D. R.; Patterson, R. L. S. Br. Veteri. J. 1974, 130, 61   DOI
13 Spinelli, S.; Vincent, R.; Pelosi, P.; Tegoni, M.; Cambillau, C. Eur. J. Biochem. 2002, 269, 2449   DOI   ScienceOn
14 Rarey, M.; Kramer, B.; Lengauer, T.; Klebe, G. J. Mol. Biol. 1996, 261, 470   DOI   ScienceOn
15 Rarey, M.; Kramer, B.; Lengauer, T. J. Comput.-Aided Mol. Des. 1997, 11, 369   DOI   ScienceOn
16 Lee, D. Y.; Hyun, K. H.; Park, H. Y.; Lee, B.-S.; Kim, C. K. Bull. Korean Chem. Soc. 2006, 27, 273   DOI   ScienceOn
17 Kim, C.; Kim, J.; Park, H.-Y.; McLean, R. J. C.; Kim, C. K.; Jeon, J.; Yi, S.-S.; Kim, Y. G.; Lee, Y.-S.; Yoon, J. J. Microbiol. Biotechnol. 2007, 17, 1598   과학기술학회마을
18 Dixon, S. L.; Koehler, R. T. J. Med. Chem. 1999, 42, 2887   DOI   ScienceOn
19 Fine, R. M.; Wang, H.; Shenkin, P. S.; Yarmush, D. L.; Levinthal, C. Proteins 1986, 1, 342   DOI   ScienceOn
20 Kim, C. K.; Lee, K. A.; Zhang, H.; Cho, H.; Lee, B.-S. Bull. Korean Chem. Soc. 2007, 28, 1141   DOI   ScienceOn