Abstract Text Bisphenol A (BPA), an endocrine disruptor or antagonist for androgen receptor (AR), has been reported to be able to inhibit male reproductive endocrine by binding with AR to form BPA-AR complex. However the molecular interaction of docking BPA to AR to form complex remained not to be better characterized. Based on previous reports, presently the study in molecular interaction find out that 12 amino acid (AA) residues from AR polypeptide chain, which are Leu701, Leu704, Asn705, Met895, Gly708, Trp741, Leu707, Arg752, Met749, Phe764, Met780 and Met742, participate in BPA-AR complex formation and make it stable by exerting the hydrophobic interactions of 11 AA residues and the hydrogen bond that the AA residue Arg752 forms with phenolic oxygen group of BPA molecule. Comparing to the molecular interactions of docking testosterone (TST), a natural androgen or agonist for its receptor, to AR to form complex, the hydrophobic interactions from two AA residues, Leu707 and Gly708, are only happening in BPA-AR complex but not in TST-AR complex. Owing to show maxium number of hydrophobic interactions with BPA molecule and loss in accessible surface area, the AA residue Leu704 is considered as an important and key interacing AA residue in BPA-AR complex. Unlike in TST-AR complex where the residue Asn705 form a hydrogen bond with TST molecule, in BPA-AR complex the residue Asn705 does not form hydrogen bond with BPA molecule except for exerting hydrophobic interaction. In addition, the score result that BPA has a higher value of Dock score than TST reveals that he BPA has stronger competitiveness than TST in binding with AR. On the other hand, the dissociation constant of BPA is lower than that of TST, suggesting that BPA-AR complex is more stable than TST-AR complex. Above molecular analysis will facilitate the sequent research on endocrine disrupting chemicals and steroid hormone receptors. Date of Presentation October 17, 2024
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