Paper
The Interaction Between 1-[p-(dimethylamino)benzoyl]-4-phenyl-Semicarbazide and Serum Albumin by Fluorescence Spectroscopy
Published 2009 · Xu Yi-min
Journal of Nanchang University
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Abstract
A new compound,1-[p-(dimethylamino)benzoyl]-4-phenyl-semicarbazide(1),had been synthesized and the interactions between 1 and bovine serum albumin(BSA) or human serum albumin(HSA) were studied by fluorescence spectroscopy.The results suggested that the fluorescence intensity of 1 increased and showed good linear relationship with the amount of BSA or HSA.1 could also quench the intrinsic fluorescence of serum albumin through static quenching procedure.The binding constants(Kb) between 1 and proteins were 4169 mol-1 L for BSA and 1 412 mol-1 L for HSA respectively,meanwhile the average number of binding sites(n) was about 1.The binding distance between 1 and BSA or HSA was evaluated on the basis of the theory of energy transfer,which indicated that BSA could transfer energy to 1 more easily,compared with HSA.In addition,the effect of 1 on the conformation of BSA/HSA was investigated by synchronous fluorescence spectroscopy which implied that 1 was close to tyrosine residue but didn't effect the conformation of protein.At the same time,the interaction between the control compound [1-[p-(dimethylamino)benzoyl]-4-phenyl-thiosemicar bazide(2)] and proteins was also investigated.The results showed neither fluorescence spectral profile nor fluorescence intensity changes of 2 were observable in the presence of HSA or BSA.Thus,it was assumed that 1 possessed strong binding ability with protein due to the amide bond of urea group which is similar to the peptide bond.The results provide the useful data for drug design and screening.
The new compound, 1-[p-(dimethylamino)benzoyl]-4-phenyl-semicarbazide(1), shows strong binding ability with serum albumin due to the amide bond of urea group, providing valuable data for drug design and screening.
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