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β- Comprehensive multispectral analysis and molecular simulation of the binding of carboline silver compound to human serum albumin

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Document pages: 11 pages

Abstract: β- Kapolin( β CS) belongs to the family of natural alkaloids, which is derived from 9h pyridine [3,4-b] indole, also known as dehydrogenated harmine (hnor). I see β The importance of CS alkaloid family in biological processes. A comprehensive binding study of four Ag (I) compounds containing ligand hnor and with different anti anions (i.e. NO3) −, chlorine dioxide −, BF4 −, and PF6 − was reported. Human serum albumin (HSA) was used as a model protein. Different methods such as UV-vis spectroscopy, fluorescence spectroscopy, circular dichroism (CD) and molecular docking have been used for this purpose. The fluorescence results show that the binding phenomenon of silver (hnor) complex with HSA can be inferred from the static quenching mechanism. The results show that the Ag (I) used has a significant binding tendency compounds towards HSA. The role of the counteranion on the binding of Ag(I) compounds to HSA appeared to be remarkable. Compounds with (ClO4−) and (NO3−) were found to have the most efficient binding towards HSA as compared to BF4−and PF6−. Circular dichroism (CD) studies made clear that conformational changes in the secondary structure of HSA were induced by the presence of Ag(I) compounds. Also, the α-helical structure of HSA was found to get transformed into a β-sheeted structure. Interestingly, (ClO4−) and (NO3−) compounds were found to induce most substantial changes in the secondary structure of HSA. The outcome of this study may contribute to understanding the propensity of proteins involved in neurological diseases (such as Alzheimer’s and Parkinson’s diseases) to undergo a similar transition in the presence of Ag-β-carboline compounds.

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