원문정보
Molecular Docking of Tetrahydrofuran-2-yl Analogues to Porcine Odorant Binding Proteins (pOBP & pPBP) and Binding Interactions
초록
영어
The binding affinity constants (p(Od)50) and molecular docking scores (DS) between porcine odorant binding proteins pOBP (1HQP) and pPBP (1GM6) as receptor and a series of tetrahydrofuran-2-yl (A & B) analogues as substrate, and their interactions were discussed quantitatively using three-dimensional quantitative structure-activity relationship (3D-QSAR) models. The statistical qualities of the optimized CoMFA models for pOBP were better than those of the CoMSIA models. The binding affinity constants and DS between substrate and receptor molecules were dependent upon steric and hydrophobic interaction. The DS constants of the substrates into the binding site of OBP (1HQP) were bigger than those of PBP (1GM6). The resulting contour maps produced by the optimized CoMFA model were used to identify the structural features relevant to the binding affinity in binding site of pOBP.
목차
서론
재료 및 방법
결합 친화력상수와 분자도킹
물리-화학 파라미터 계산
3D-QSAR 모델의 유도
부분최소 자승(PLS) 계산
결과
결합 친화력과 DS
pOBP에 대한 QSAR 모델
DS에 대한 QSAR 모델
고찰
결합 친화력상수와 QSAR 모델
기질-수용체 등고도 분석
도킹 스코어와 QSAR 모델
결합 친화력상수와 QSAR 모델
기질-수용체 상호작용
인용문헌