4.7 Article

Conformational Changes in the BSA-LT4 Complex Induced by the Presence of Vitamins: Spectroscopic Approach and Molecular Docking

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出版社

MDPI
DOI: 10.3390/ijms23084215

关键词

vitamins; BSA-LT4 complex; spectroscopy; molecular docking

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  1. Romanian Ministry of Research and Innovation, CCCDI-UEFISCDI [PN-III-P1-1.2-PCCDI-2017-0062, 58]

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Levothyroxine (LT4) is commonly used for treating hypothyroidism. This study investigated the influence of vitamins (C, B12, and folic acid) on the complex of Bovine Serum Albumin with LT4 (BSA-LT4). The results showed that vitamin C and folic acid statically quenched the fluorescence of the BSA-LT4 complex, while vitamin B12 had a combined mechanism. The binding of vitamin B12 was stronger, resulting in an extended storage time of LT4 in blood plasma. The interaction between the vitamins and BSA-LT4 mainly occurred near Trp, with vitamin B12 having the most pronounced effect.
Levothyroxine (LT4) is known for its use in various conditions including hypothyroidism. LT4 interaction with serum albumin may be influenced by the presence of vitamins. For this reason, we investigated the effect of vitamin C, vitamin B12, and folic acid on the complex of Bovine Serum Albumin with LT4 (BSA-LT4). UV-Vis spectroscopy was used to monitor the influence of vitamins on the BSA-LT4 complex. Fluorescence spectroscopy revealed a static quenching mechanism of the fluorescence of BSA-LT4 complex by the vitamin C and folic acid and a combined mechanism for vitamin B12. The interaction of vitamin C and folic acid with BSA-LT4 was moderate, while the binding of vitamin B12 was much stronger, extending the storage time of LT4 in blood plasma. Synchronous fluorescence found that the vitamins were closer to the vicinity of Trp than to Tyr and the effect was more pronounced for the binding of vitamin B12. The thermal stability of the BSA-LT4 complex was more evident, but no influence on the stability of BSA-LT4 complex was obtained for vitamin C. Molecular docking studies showed that vitamin C and folic acid bound the same site of the protein, while vitamin B12 bonded to a different site.

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