By a News Reporter-Staff News Editor at Biotech Week -- Investigators discuss new findings in Drugs and Therapies. According to news reporting out of Riyadh, Saudi Arabia, by NewsRx editors, research stated, "In this report we have studied the interaction of sulfadiazine (SD), which has recently been found to partially protect the amyloidosis, with human serum albumin (HSA) at physiological conditions of temperature and pH. We have employed several basic and advanced spectroscopic techniques such as UV, fluorescence, circular dichroism (CD) and Fourier transform infra-red (FTIR) spectroscopies."
Our news journalists obtained a quote from the research from King Saud University, "UV spectrum of native HSA was different from the spectrum of HSA in the presence of SD due to the complex formation between albumin and drug. Fluorescence quenching of HSA by SD at 280 nm was due to the formation of HSA-SD complex. The data were analyzed using Stern-Volmer (SV) and the quenching was found to be static with 1:1 binding ratio. Synchronous fluorescence spectra have shown a red shift and revealed that hydrophobicity around both Trp and Tyr residues was decreased. CD results have shown that the conformation of macromolecule remains undisturbed at low concentrations (up to 20 mu M of the SD), though, a small change in the secondary structure from 20 to 75 mu M of SD was observed followed by a large change and consequent unfolding on further increase in the drug concentration. Both synchronous and CD measurements were consistent to each other."
According to the news editors, the research concluded: "From the FTIR measurement analysis it was found that amide I band also shifted which concluded that the conformational changes take place in the presence of SD."
For more information on this research see: Interaction of human serum albumin with sulfadiazine. Journal of Molecular Liquids, 2014;197():124-130. Journal of Molecular Liquids can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands. (Elsevier - www.elsevier.com; Journal of Molecular Liquids - www.elsevier.com/wps/product/cws_home/500849)
Our news journalists report that additional information may be obtained by contacting M.S. Ali, King Saud Univ, Dept. of Chem, Surfactant Res Chair, Riyadh 11451, Saudi Arabia (see also Drugs and Therapies).
Keywords for this news article include: Riyadh, Saudi Arabia, Asia, Acute-Phase Proteins, Blood Proteins, Drugs, Drugs and Therapies, Organic Chemicals, Pharmaceuticals, Serum Albumin, Sulfadiazine, Sulfanilamides, Sulfones, Sulfur Compounds, Therapy
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