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Issue 3, 2021

Ex vivo binding studies of the anti-cancer drug noscapine with human hemoglobin: a spectroscopic and molecular docking study

Author affiliations

Abstract

Noscapine is a non-narcotic alkaloid known to display anti-cancer activity against a wide variety of tumors. Since plasma proteins play the central role in drug transport and targeting, herein we study the binding of noscapine hydrochloride (Nos) with human hemoglobin (Hb), a naturally encapsulated transport molecule. The molecular and biophysical basis of Nos–Hb binding has been investigated by using UV-vis, fluorescence spectroscopy, circular dichroism (CD) and computational methods. The Benesi–Hildebrand binding constant (Kb) and Stern–Volmer constant (KSV) were determined to be 150 M−1 and 5.31 × 103 M−1, respectively. The biomolecular-quenching constant (Kq), 1.06 × 1012 M−1 s−1, indicated a rather static quenching mechanism and negative value for free energy (ΔG −12.5 kJ M−1) which suggests the feasible interaction of Nos with Hb. Job's plot indicates a 1 : 1 binding stoichiometry for Hb–Nos interaction. CD and FTIR spectroscopy studies dictate a change in the secondary structure of Hb upon its interaction with Nos. FRET analysis calculates a distance of 7 nm between Hb and Nos and also confirms the energy transfer between them. Molecular docking studies verified the interacting amino acids and atoms of the Hb–Nos complex and its stability.

Graphical abstract: Ex vivo binding studies of the anti-cancer drug noscapine with human hemoglobin: a spectroscopic and molecular docking study

Supplementary files

Article information


Submitted
02 Jul 2020
Accepted
26 Nov 2020
First published
07 Dec 2020

New J. Chem., 2021,45, 1525-1534
Article type
Paper

Ex vivo binding studies of the anti-cancer drug noscapine with human hemoglobin: a spectroscopic and molecular docking study

H. Chugh, P. Kumar, N. Kumar, R. K. Gaur, G. Dhawan and R. Chandra, New J. Chem., 2021, 45, 1525 DOI: 10.1039/D0NJ03334K

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