NEW METHOD FOR PREDICTING BINDING-AFFINITY IN COMPUTER-AIDED DRUG DESIGN

被引：1041

作者：

AQVIST, J ^{[1
]}

MEDINA, C ^{[1
]}

SAMUELSSON, JE ^{[1
]}

机构：

[1] SYMBICOM AB,S-75183 UPPSALA,SWEDEN

来源：

PROTEIN ENGINEERING | 1994年 / 7卷 / 03期

关键词：

BINDING FREE ENERGIES; DRUG DESIGN; ENDOTHIAPEPSIN; INHIBITOR BINDING; MOLECULAR DYNAMICS SIMULATION;

D O I：

10.1093/protein/7.3.385

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A new semi-empirical method for calculating free energies of binding from molecular dynamics (MID) simulations is presented. It is based on standard thermodynamic cycles and on a linear approximation of polar and non-polar free energy contributions from the corresponding Mn averages. The method is tested on a set of endothiapepsin inhibitors and found to give accurate results both for absolute as well as relative free energies.

引用

页码：385 / 391

页数：7

共 37 条

[1]

AQVIST J, 1990, J PHYS CHEM-US, V94, P8021, DOI 10.1021/j100384a009

[2]

AQVIST J, 1993, J AM CHEM SOC, V115, P631

[3] CALCULATION OF THE RELATIVE CHANGE IN BINDING FREE-ENERGY OF A PROTEIN-INHIBITOR COMPLEX [J].