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Free Energy Calculations of HIV-1 Protease Binding Indinavir and Its Drug-Resistant Mutant
https://repo.qst.go.jp/records/80520
https://repo.qst.go.jp/records/80520e46d3071-a571-44b4-9643-4a3008637902
| アイテムタイプ | 会議発表用資料 / Presentation(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2020-06-11 | |||||
| タイトル | ||||||
| タイトル | Free Energy Calculations of HIV-1 Protease Binding Indinavir and Its Drug-Resistant Mutant | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_c94f | |||||
| 資源タイプ | conference output | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
Taguchi, Masahiko
× Taguchi, Masahiko× Oyama, Ryo× Kaneso, Masahiro× Hayashi, Shigehiko× Taguchi, Masahiko |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | HIV-1 protease is a target of drug development and various inhibitors binding to two Asps in the catalytic site were developed. However, it has a serious drug-resistance, that is, some mutations cause existing inhibitors ineffective, even though hydrolysis reaction of substrate proceeds. To resolve the drug-resistance problem, it is important to clarify difference of recognition mechanism of the protease for inhibitors in the case of native and drug resistance mutational structures, respectively. For indinavir, it is known that mutation (V82T/I84V) greatly affects its binding free energy to HIV-1 protease. We performed QM/MM free energy calculations, and succeeded to determine the protonated states of catalytic Asps and the relative binding free energy. | |||||
| 会議概要（会議名, 開催地, 会期, 主催者等） | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 第58回日本生物物理学会年会 | |||||
| 発表年月日 | ||||||
| 日付 | 2020-09-16 | |||||
| 日付タイプ | Issued | |||||
