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Abstract In this study, the binding characteristics of aloe-emodin (AE) and pepsin were investigated via multiple spectroscopic and molecular docking methods. The Stern-Volmer quenching constant (Ksv) suggested that AE quenched… Click to show full abstract
Abstract In this study, the binding characteristics of aloe-emodin (AE) and pepsin were investigated via multiple spectroscopic and molecular docking methods. The Stern-Volmer quenching constant (Ksv) suggested that AE quenched the fluorescence intensity of pepsin via static quenching. The value of the stoichiometric binding number (n) suggested only a single binding site on pepsin for AE. The value of Gibbs’ free energy change (ΔG)
Keywords:
pepsin;
characteristics aloe;
spectroscopy;
emodin pepsin;
aloe emodin;
binding characteristics
Journal Title: Journal of Molecular Structure
Year Published: 2019
Link to full text (if available)
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Journal Title: Journal of Molecular Structure
Year Published: 2019
Link to full text (if available)
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recommendations!