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The bioinformatics method is used to analyze the relationship of serum albumin among different species, and to analyze the characteristics of the amino acid changes in the other closely related species of the interaction sites of hypoglycemic drugs miglitol and voglibose with human serum albumin. The results show that the binding sites of miglitol, voglibose and human serum albumin are located at the hydrophobic cavity of human serum albumin subdomain IB, and the main forces are hydrogen bonding and hydrophobic interaction. The amino acids at the binding sites of miglitol and voglibose with human serum albumin are mostly conserved in other species, with only a few amino acids being different and polarities being different. The serum albumin hydrophobicity analysis suggests that the amino acids at the binding sites of miglitol and voglibose with serum albumin are more hydrophilic, less hydrophobic, and the other four species in the same species also have the same phenomenon. These bioinformatics based analysis provide an important scientific basis for the further research on the expression and interaction of hypoglycemic drugs in other species. [ABSTRACT FROM AUTHOR]

Recently, curcumol is one of the important new anti-tumor traditional Chinese medicine monomer. It can help us to better understand the mechanism of drug's action by analyzing the interaction between curcumol and transporter-serum albumin. In this paper, we analyzed the molecular interaction between curcumol and human serum albumin, as well as the characteristics in other closely related species by using multiple sequence analysis, evolutionary relationship and molecular docking technique. The results showed that the active sites II and III between curcumol and human serum albumins are surrounded by hydrophobic amino acids, which suggested that intermolecular hydrophobic interaction plays a very important role. Their lowest binding energies are -7.22 kcal/mol and -8.34 kcal/mol, respectively. Most of the amino acids in the active sites are conservative in other close genetic species, such as Canis lupus, Ovine, Bos mutus and Bos Taurus. It is noticed that few changes occurred between the amino acids with identical polarity. The conformation of the hydroxyl group in curcumol has the most obvious variation in the active site compared with the optimal structure. [ABSTRACT FROM AUTHOR]