Multispectroscopic and computational study of interaction of the bovine serum albumin with atropine and atropine-loaded chitosan nanoparticles (synthesized and characterized).

Two different systems of bovine serum albumin (BSA) were used for multiple spectroscopic and computational studies to determine interaction of BSA and atropine (Atrop), that is, BSA-Atrop system and Atrop-loaded chitosan nanoparticles (Atrop@CS NPs), that is, BSA-Atrop@CS NPs system. The study suggests that BSA-Atrop system and BSA-Atrop@CS NPs system involve non-fluorescent complexes of  = 3.2 × 10 Lmol and 3.

Binding ability of roxatidine acetate and roxatidine acetate supported chitosan nanoparticles towards bovine serum albumin: characterization, spectroscopic and molecular docking studies.

The RxAc drug loaded on Tween80-chitosan-TPP nanoparticles (NRxAc) has been characterized and probed by UV-Vis, PXRD, FTIR, DLS and SEM technique. The physicochemical characteristics of NRxAc have been employed and evaluated for formulation of drug, particle size, external morphology, drug content and in vitro drug release. Multi-spectroscopic (i.

Effect of local anesthetic drug procaine hydrochloride on the conformational stability of bovine hemoglobin: Multi-spectroscopic and computational approaches.

The interaction between bovine hemoglobin (BHb) and local anesthetic drug procaine hydrochloride (PCH) was examined by spectroscopic and computational studies. Intrinsic fluorescence analysis explored the ground-state complex formation in the binding of PCH with BHb through static quenching mechanism. The binding constants () are 29.

Exploring the intermolecular interactions and contrasting binding of flufenamic acid with hemoglobin and lysozyme: A biophysical and docking insight.

The intermolecular interaction of flufenamic acid (Hfluf) with two model proteins i.e., hemoglobin and lysozyme was explored using fluorescence, UV-vis, circular dichroism, DLS, and molecular docking techniques.

Probing the intermolecular interactions into serum albumin and anthraquinone systems: a spectroscopic and docking approach.

Intermolecular interaction study of human serum albumin (HSA) with two anthraquinones i.e. danthron and quinizarin has been performed through fluorescence, UV-vis and CD spectroscopy along with docking analysis.