Spectroscopic analyses on interaction of o-Vanillin-d-Phenylalanine, o-Vanillin-l-Tyrosine and o-Vanillin-l-Levodopa Schiff Bases with bovine serum albumin (BSA)
作者： Jingqun Gao , Yuwei Guo , Jun Wang , Zhiqiu Wang , Xudong Jin
DOI: 10.1016/J.SAA.2010.12.077
关键词:
摘要: Abstract In this work, three o-Vanillin Schiff Bases (o-VSB: o-Vanillin- d -Phenylalanine (o-VDP), l -Tyrosine (o-VLT) and -Levodopa (o-VLL)) with alanine constituent were synthesized by direct reflux method in ethanol solution, then used to study the interaction bovine serum albumin (BSA) molecules fluorescence spectroscopy. Based on quenching calculation, bimolecular constant (Kq), apparent (Ksv), effective binding (KA) corresponding dissociation (KD) as well site number (n) obtained. addition, distance (r) was also calculated according Foster's non-radioactive energy transfer theory. The results show that these o-VSB can efficiently bind BSA molecules, but array order is o-VDP-BSA > o-VLT-BSA > o-VLL-BSA. Synchronous spectroscopy indicates o-VDP more accessibility tryptophan (Trp) residues of than tyrosine (Tyr) residues. Nevertheless, o-VLT o-VLL are Tyr Trp
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