Protein-ligand interaction energy analysis between anti-trypanosome drug candidate and target protein using fragment molecular orbital

• Ryunosuke Yoshino

  Global Scientific Information and Computing Center, Tokyo Institute of Technology

• Nobuaki Yasuo

  Department of Computer Science, Tokyo Institute of Technology

• Yohsuke Hagiwara

  Chemistry Research Labs, Drug Discovery Research, Astellas Pharma Inc

• Kazuki Ohno

  Chemistry Research Labs, Drug Discovery Research, Astellas Pharma Inc

• Masaya Orita

  Global Scientific Information and Computing Center, Tokyo Institute of Technology | Chemistry Research Labs, Drug Discovery Research, Astellas Pharma Inc

• Masayuki Inoue

  Graduate School of Pharmaceutical Sciences, The University of Tokyo

• Shigeharu Harada

  Graduate School of Science and Technology, Kyoto Institute of Technology

• Teruki Honma

  Graduate School of Medicine, The University of Tokyo

• Daniel KenInaoka

  Graduate School of Medicine, The University of Tokyo

• Kiyoshi Kita

  Graduate School of Medicine, The University of Tokyo

• Masakazu Sekijima

  Global Scientific Information and Computing Center, Tokyo Institute of Technology | Department of Computer Science, Tokyo Institute of Technology

Bibliographic Information

Other Title

• FMO法を用いた抗トリパノソーマ候補薬と標的蛋白質間の相互作用解析

Abstract

Chagas' disease caused by Trypanosoma cruzi is known as neglected tropical diseases (NTD's). To develop effective anti-Trypanosome drug, we remarked dihydroorotate dehydrogenase which assumed synthesis of orotic acid and studied inhibitor of the enzyme. Although X-ray structure of target protein with inhibitor is clarified, important protein-ligand interaction is not determined for elucidation of inhibition mechanism. Then, in this research, we analyzed interaction energy between target proteins and inhibitors using fragment molecular orbital method. As a result, it was revealed that hydrogen bonding with Lys and Asn was important. It is expected that these results are useful for anti-Trypanosome drug design.

Journal

• IPSJ SIG technical reports

  IPSJ SIG technical reports 2013 (5), 1-7, 2013-12-04

  Information Processing Society of Japan (IPSJ)

Details

• CRID: 1573668927652772992
• NII Article ID: 110009634027
• NII Book ID: AA12055912
• ISSN: 09196072
• Text Lang: ja
• Data Source:
  • CiNii Articles