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.

ABSTRACT   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

• 조윤기(충남대학교 농업생명과학대학 응용생물환경화학과) | Yun-Gi Cho
• 박창식(충남대학교 형질전환복제돼지연구센터) | Chang-Sik Park
• 성낙도(충남대학교 농업생명과학대학 응용생물환경화학과) | Nack-Do Sung Corresponding author