In vitro Analysis of the Interaction between Human Serum Albumin and Semi-Synthetic Clerodanes

Journal of the Brazilian Chemical Society

Chaves, Otávio A.¹  Echevarria, Áurea² 

[1] Universidade Federal Rural do Rio de Janeiro, Seropédica, Brazil;Universidade Federal do Rio Grande do Norte, Natal, Brazil

关键词: Croton cajucara;    trans-dehydrocrotonin derivatives;    human serum albumin;    spectroscopy;    molecular docking.;   

DOI  :  10.21577/0103-5053.20180054

学科分类：化学（综合）

来源: SciELO

【 摘 要 】

The interaction between HSA and two semi-synthetic potential anti-cancer agents derived from trans -dehydrocrotonin-methyl-hydrazone (MHDCTN) and phenyl-hydrazone (PHDCTN) was evaluated under physiological conditions at 296, 303 and 310 K by multi-spectroscopic techniques and molecular docking calculations. Steady state fluorescence quenching indicated a ground state association (static quenching) for both samples; however, the quenching induced by PHDCTN was not essentially static and can be accompanied by a dynamic quenching mechanism. The binding is strong (modified Stern-Volmer binding constant (Ka) ca. 105 M-1), causing a very weak perturbation on the secondary structure of the protein and there is just one main binding site for both samples (Sudlow’s site I). Molecular docking results suggested hydrogen bonding and hydrophobic interactions as the main binding forces for both samples.

【 授权许可】

CC BY