Comparative studies on the interactions between human serum albumin, bovine serum albumin and cholesterol: ftir and fluorescence spectroscopy

dc.contributor.author S., Abu Sharkh
dc.contributor.author H., Alsamamra
dc.contributor.author S.M., Darwish
dc.contributor.author M. M., Abu Teir
dc.date.accessioned 2019-12-09T12:11:04Z
dc.date.available 2019-12-09T12:11:04Z
dc.date.issued 2018-07-30
dc.description.abstract The interaction of the human serum albumin (HSA), bovine serum albumin (BSA) with cholesterol has been investigated. The basic binding interaction was studied by FTIR and fluorescence spectroscopy. From spectral analysis cholesterol showed a strong ability to quench the intrinsic fluorescence of HSA and BSA through a static quenching mechanism. The binding constant (k) between HSA and cholesterol is estimated to be K=2.14 × 103 M-1 at 293 K while between BSA and cholesterol is estimated to be K=.1.12 × 103 M-1 at the same temperature. FTIR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure and cholesterol binding mechanisms. The observed spectral changes indicate a higher percentage of H-bonding between cholesterol and -helix compared to the percentage of H-bonding to cholesterol and -sheets. en_US
dc.description.sponsorship This work is supported by the German Research Foundation DFG grant No. DR228/24-2 en_US
dc.identifier.citation Asian Journal of Science and Technology en_US
dc.identifier.issn 0976-3376
dc.identifier.uri https://dspace.alquds.edu/handle/20.500.12213/4998
dc.language.iso en en_US
dc.subject BSA en_US
dc.subject HSA en_US
dc.subject binding constant en_US
dc.subject IR and Fluorescence Spectroscopy en_US
dc.title Comparative studies on the interactions between human serum albumin, bovine serum albumin and cholesterol: ftir and fluorescence spectroscopy en_US
dc.type Article en_US
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