作者: Shahper Khan , Barira Islam , M Rajeswari , Hammad Usmani , Asad Khan
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摘要: Thiopental (TPL) is a commonly used barbiturate anesthetic. Its binding with human serum albumin (HSA) was studied to explore the anesthetic-induced protein dysfunction. The basic interaction by UV-absorption and fluorescence spectroscopy. An increase in affinity (K) number of sites (n) increasing concentration observed. conformation-dependent highest for F isomer HSA, which implicates its slow elimination. mode characterized using various thermodynamic parameters. Domain II HSA found possess high site TPL. effect micro-metal ions on also investigated. molecular distance, r, between donor acceptor estimated resonance energy transfer (FRET). Correlation stability TPL-N TPL-F complexes drug distribution discussed. structural changes investigated circular dichroism (CD) Fourier transform infrared (FT-IR) spectroscopy reflect perturbation molecule provide an explanation heterogeneity action this