Spectroscopic and computational investigation of the interaction between the new anticancer agent enasidenib and human serum albumin.

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Saber Abdelhameed A, Bakheit AH, Hassan ES, Alanazi AM, Naglah AM, AlRabiah H

Spectroscopic and computational investigation of the interaction between the new anticancer agent enasidenib and human serum albumin.

Spectrochim Acta A Mol Biomol Spectrosc. 2022 Apr 5;270:120790. doi: 10.1016/j.saa.2021.120790. Epub 2021 Dec 22.

PubMed ID

34974294 [ View in PubMed

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Abstract

Enasidenib (EDB) is a new therapeutic agent for the treatment of adult patients with relapsed or refractory acute myeloid leukemia (AML) with an isocitrate dehydrogenase-2 (IDH2) mutation. This research aimed at utilizing experimental and theoretical approaches to characterize the binding mechanism between EDB and human serum albumin (HSA). Formation of an EDB-HSA static complex was demonstrated by quenching of the HSA intrinsic fluorescence by EDB. Using well known mathematical relations (e.g. Stern-Volmer and Lineweaver-Burk equations), the recorded EDB-HSA fluorescence data were interpreted and revealed binding constants in the magnitude order of 10(4) M(-1) for the different investigated temperatures. These determined results were taken into further mathematical calculations to reveal the thermodynamic properties of EDB-HSA binding. Results demonstrated that spontaneous EDB and HSA binding takes place led by electrostatic forces. Computational docking studies have further confirmed the latter finding showing that EDB fits into the HSA Sudlow site I. Molecular dynamic simulation was performed to calculate the root mean square deviation (RMSD), root mean square fluctuation (RMSF), radius of gyration (R(g)) and hydrogen bond parameters for the EDB-HSA complex.

DrugBank Data that Cites this Article

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Enasidenib	Serum albumin	Protein	Humans	No	Binder	Details