Estimation of ligand receptor binding affinity from the fluctuation of their interface 

作成者 Iwamoto, Koji, Ode, Hirotaka, Ohta, Masami, Misu, Takashi, Hata, Masayuki, Neya, Saburo, Hoshino, Tyuji
作成者の別表記 畑, 昌之, 根矢, 三郎, 星野, 忠次
キーワード等 binding energy, drug design, computation, affinity, interface
日本十進分類法 (NDC) 490
内容 It is necessary for the understanding of protein interactions or in silico drug designs to accurately estimate ligand-receptor affinity. The energy calculation based on the electrostatic force, van der Waals force, and solvation effect is a direct method of computing the magnitude of the interaction between ligand and receptor. By this conventional method, however, it is difficult to estimate a slight difference in binding affinity with sufficient accuracy. We propose a novel concept for the evaluation of binding affinity between a ligand and its receptor by functionalizing the fluctuation at the ligand-receptor interface. This method enables an adequate estimation with a high accuracy compared with the conventional energetic approach. Human immunodeficiency virus type 1 (HIV-1) protease and its inhibitor are used to explain how binding affinity is extracted from the fluctuation in interfacial energy, and a combination of an antigen and its antibody is examined to demonstrate the compatibility between the estimation from the interfacial fluctuation and the experimentally measured binding energy.
作成日付 2005-10-21
コンテンツの種類 雑誌掲載論文 Journal Article
DCMI資源タイプ text
ファイル形式 application/pdf
ISSN 0021-4922
NCID AA10457675
掲載誌情報 Japanese Journal of Applied Physics Vol.44 no.44 page.L1370-L1372 (2005-10-21)
言語 英語
著者版フラグ author

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