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Morphological changes in human serum albumin in presence of cationic amphiphilic drugs

Abstract

Human serum albumin (HSA) is one of the most important carrier proteins present in the blood and can constitute more than half of serum proteins. It transports various biomolecules including hormones, fatty acids, ions, drugs and functions to regulate oncotic pressure in the plasma. Cationic amphiphillic drugs like amitriptyline hydrochloride, imipramine hydrochloride and promethazine hydrochloride bind to HSA and influences function by altering its conformation, as confirmed by Small-angle neutron scattering (SANS) data coupled to dynamic light scattering measurements (DLS). Protein unfolding was observed by SANS results through an increase in the value of the radius of gyration Rg. At higher drug concentrations, there was no change in the dimensions of the protein. However, the drugs formed free aggregates at higher concentrations without any growth in the drug micelles, which was confirmed by the appearance of second peak in DLS measurements. Molecular docking revealed that the morphology of hydrophobic moiety of the cationic amphiphilic drugs decides their binding fate with HSA, while trajectories from molecular dynamics simulations highlight structural disorder in the drug-HSA complex.

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Publication details

The article was received on 16 Jul 2017, accepted on 04 Jan 2018 and first published on 05 Jan 2018


Article type: Paper
DOI: 10.1039/C7NJ02591B
Citation: New J. Chem., 2018, Accepted Manuscript
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    Morphological changes in human serum albumin in presence of cationic amphiphilic drugs

    Z. Yaseen, V. K. Aswal, X. Zhou, . Kabir-ud-Din and S. Haider, New J. Chem., 2018, Accepted Manuscript , DOI: 10.1039/C7NJ02591B

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