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Natural Science, Biology, 2024, 14, 67–75
DOI: 10.xxxx/example-doi Special Issue 1(2), 2022 186–1928

QUENCHING MECHANISM OF HUMAN SERUM ALBUMIN FLUORESCENCE BY GANGLERON

Received N/A; revised N/A; accepted N/A
CC BY-NC 4.0 This work is licensed under Creative Commons Attribution–NonCommercial International License (CC BY-NC 4.0).

Interaction between Gangleron (spasmolytic and anaesthetizing drug) and human serum albumin (HSA) was studied using UV/vis and fluorescence spectroscopy methods. The quenching mechanism of HSA fluorescence was discussed based on interaction studies carried out at different temperatures (298, 303 and 309 K). Stern-Volmer constant (KSV), quenching rate constant (kq) and activation energy of bimolecular quenching (Еа) were evaluated. UV/vis absorption spectra were used to confirm the quenching mechanism.

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