Journal
ACS APPLIED BIO MATERIALS
Volume 2, Issue 8, Pages 3551-3561Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsabm.9b00429
Keywords
olanzapine-NBD derivative; human serum albumin; beta-cyclodextrin; static quenching; circular dichroism; association kinetics; molecular docking
Funding
- DST, West Bengal [809(Sanc)/ST/P/ST/4G-9/2104]
- CSIR, New Delhi, India [01(2896)/17/EMR-II]
- UGC-NET Fellowship (SRF) UGC, New Delhi, India
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Here, we present a detailed investigation on the interaction of 4-chloro-7-nitro-1,2,3-benzoxadiazole (NBD) embedded olanzapine derivative (OLA-NBD) with a model transport protein, human serum albumin (HSA). The thermodynamic parameters, Delta Ho degrees, Delta So degrees, and Delta Go degrees, as evaluated by considering the van't Hoff relationship imply the major contribution of electrostatic/ionic interactions for the HSA-OLA-NBD association. The OLA-NBD induced quenching of HSA emission occurs through static quenching mechanism, indicating a 1:1 association, as portrayed from Benesi-Hildebrand plot, with similar to 10(4) M-1 association constant value, and it is in good harmony with the value estimated from anisotropy experiment. The invariance of the time-resolved decay behavior of HSA with added OLA-NBD concentration, along with matching dependency of the binding constant (K-b) value on temperature, also supports the occurrence of static quenching. The effect of beta-cyclodextrin on HSA-OLA-NBD binding is characterized by a smaller K-b value revealing that the OLA-NBD molecules are gradually removed from beta-CD by HSA to achieve its medicinal outcome of drug delivery. The outcome from circular dichroism (CD) illustrates the variation of HSA secondary structure upon interaction with OLA-NBD. Concurrently, HSA-OLA-NBD association kinetics is also explored by applying the fluorescence technique. The possible interaction zone of OLA-NBD in HSA is investigated from AutoDock-based docking simulation study.
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