Investigation of the Binding Interaction of α -Amylase with Chrysophyllum albidum Seed Extract and its Silver Nanoparticles: A Multi-Spectroscopic Approach
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Date
2020
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ELSEVIER Chemical Data Collections
Abstract
The interactions between α-amylase, one of the key enzymes linked with postprandial glucose
regulation, and Chrysophyllum albidum seed methanolic extract(CSME) and its greensynthesized silver
nanoparticles(CSAgNP) were investigated using multiple spectroscopy including Fourier Transform Infrared(FT-IR), ultraviolet(UV)-visible absorption, fluorescence spectroscopy, and biochemical analysis.
FT-IR spectroscopy revealed presence of some functional groups in the samples. CSME and CSAgNP
inhibited α-amylase. The intrinsic fluorescence intensity of α-amylase was quenched by CSME and
CSAgNP via static mechanisms, indicating formation of complex between the enzyme and inhibitors. α AmylaseCSAgNP complex had higher binding constants. The binding processes were exothermic,
entropy driven, spontaneous, and involved hydrogen bonds and van der Waals force. Synchronous
fluorescence quenching indicated alteration in microenvironment of α-amylase catalytic site tyrosine
residues. FT-IR spectroscopy revealed shifts in amide I peak position of α-amylase due to interaction
with CSME/CSAgNP. Absorption spectroscopy also affirmed changes in enzyme conformation. This study
may provide theoretical basis for designing novel α-amylase inhibitors.
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Keywords
Chrysophyllum albidum, Silver nanoparticles, α-Amylase inhibition, Protein-ligand binding interaction, Fluorescence quenching, Spectroscopy