Binding of Drug Pamabrom to Human Hemoglobin: Structural and Thermodynamic Characterization Studies

Binding of drug with human hemoglobin (HHb) and Pamabrom (PABr) have been systematically investigated by fluorescence spectroscopy, UV-visible absorption spectroscopy and synchronous spectroscopy under similar to human physiological conditions. The quenching mechanism was investigated with the quenching type, the association constants, the number of binding sites and basic thermodynamic parameters. The present paper review the drugHHb interactions, their types and applications of experimental techniques used to study interactions between HHb and small ligand molecules that are potentially of pharmaceutical interest. In summary the experimental observations indicates that interaction between HHb and PABr from complex with one binding site. In binding process hydrophobic interaction provides major role. The binding study of drug receive information about study of drug binding to physiologically important hemeprotein HH b is greatly important for regarding in pharmacy, biochemistry which provides some references for the rational use of drugs in the clinic and helpful for the clarifying the function of HHb as drug storage. Thermodynamic parameters indicate that interaction reaction is spontaneous and entropy is utilised. The study of interaction between PABr and HHb is of significant and scientific and technological important. Drugs interactions at protein binding level would significantly affect the apparent distribution volume of the drugs and also affect the elimination rate of drugs. Therefore, investigating the interaction of drugs and hemeprotein was significant for knowing the transport and distribution of drugs in body, and for clarifying the action mechanism and pharmaceutical dynamics.