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Binding studies of ferrocene‐steroid conjugates with human serum albumin as potential drug carrier using fluorescence spectroscopy and in silico docking approach
Author(s) -
NarváezPita Xiomara,
Meléndez Enrique
Publication year - 2021
Publication title -
applied organometallic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.53
H-Index - 71
eISSN - 1099-0739
pISSN - 0268-2605
DOI - 10.1002/aoc.6344
Subject(s) - chemistry , human serum albumin , docking (animal) , in silico , ferrocene , hydrophobic effect , quenching (fluorescence) , autodock , fluorescence spectroscopy , fluorescence , steroid , combinatorial chemistry , biochemistry , medicine , physics , nursing , electrode , quantum mechanics , electrochemistry , gene , hormone
The interactions of 16‐ferrocenylidene‐3α‐hydroxy androstan‐17‐one ( 1 ), 16‐ferrocenylidene‐3β‐hydroxy androstan‐17‐one ( 2 ), 21‐ferrocenylidene‐3β‐hydroxy pregn‐5‐en‐20‐one ( 3 ), and 16‐ferrocenylidene‐3β‐hydroxydehydro androstan‐17‐one ( 4 ) with human serum albumin (HSA) have been studied by fluorescence quenching spectroscopy and in silico docking calculations. The experimental results showed that the intrinsic fluorescence of HSA is quenched upon addition of the ferrocene‐steroid conjugates and the quenching mechanism is static. Thermodynamic parameters demonstrated that the protein‐ferrocene interactions are spontaneous, highly entropic, and hydrophobic. Protein‐ligand docking studies were performed using AutoDock Vina Program. Docking studies corroborated the experimental data, and the binding interactions are hydrophobic. All ferrocene‐steroid conjugates get engaged in hydrophobic interactions with LEU387, TYR411, LEU430, and ARG485 amino acid residues.