A quantitative Secondary Structure analysis of BSA on Interaction with Oseltamivir phosphate by FT-IR Spectroscopy
عنوان مقاله: A quantitative Secondary Structure analysis of BSA on Interaction with Oseltamivir phosphate by FT-IR Spectroscopy
شناسه ملی مقاله: MIAUCHEMISTRY01_148
منتشر شده در همایش منطقه ای شیمی در سال 1389
شناسه ملی مقاله: MIAUCHEMISTRY01_148
منتشر شده در همایش منطقه ای شیمی در سال 1389
مشخصات نویسندگان مقاله:
Tahereh Sadigh Vishkaee - Department of Chemistry, Azad University, Central Tehran Branch (IAUCTB), ۱۴۶۷۶ ۸۶۸۳۱, Iran
Shohreh Nafisi
خلاصه مقاله:
Tahereh Sadigh Vishkaee - Department of Chemistry, Azad University, Central Tehran Branch (IAUCTB), ۱۴۶۷۶ ۸۶۸۳۱, Iran
Shohreh Nafisi
Serum albumin are the major soluble protein constituents of the circulatory system and have many physiological functions including transporting a variety of compounds. The availability, high purity at reasonable cost of BSA and homologue structure with HSA, has made this protein favorite for study by chemists. Oseltamivir phosphate (OP; Tamiflu) is a prodrug of the anti-influenza neuraminidase inhibitor and has been developed for the treatment and prevention of both A and B strains of influenza. Infrared spectroscopy is one of the oldest and well established experimental techniques for the analysis of secondary structure of polypeptides and proteins. It is convenient, non-destructive, requires less sample preparation, and can be used under a wide variety of physical conditions. The polypeptide repeat units give rise to nine characteristic IR absorption bands, namely, amide A, B, and I-VII. The most sensitive spectral region to the protein secondary structural components is the amide I band (1600-1700 cm-1), which is due almost entirely to the C=O stretch vibrations of the peptide linkages. This study was designed to stability protein secondary structure by Fourier self-deconvolation and second-derivative analysis .The protein secondary structure showed no major alterations at low ligand concentrations (5µM), whereas at higher content (0.5 mM), decrease of α-helix from 63%(free BSA) to 41% and increase of β-sheet from 16%(free BSA) to 25% and Turn5% (free BSA) to 21% occurred in the ligand-BSA complexes. These observations indicated that low drug content induced protein stabilization (folding), whereas, at high drug concentration, a partial protein destabilization (unfolding) occurred in these drug-BSA complexes.
کلمات کلیدی: Bovine serum albumin; protein; Oseltamivir phosphate; Secondary structure; FT-IR.
صفحه اختصاصی مقاله و دریافت فایل کامل: https://civilica.com/doc/829018/