摘要
It remains challenging to develop methods that can precisely control the self-assembling kinetics and thermodynamics of peptide hydrogelators to achieve hydrogels with optimal properties.Here we report the hydrogelation of peptide hydrogelators by an enzymatically induced pH switch,which involves the combination of glucose oxidase and catalase with D-glucose as the substrate,in which both the gelation kinetics and thermodynamics can be controlled by the concentrations of D-glucose.This novel hydrogelation method could result in hydrogels with higher mechanical stability and lower hydrogelation concentrations.We further illustrate the application of this hydrogelation method to differentiate different D-glucose levels.
It remains challenging to develop methods that can precisely control the self-assembling kinetics and thermodynamics of peptide hydrogelators to achieve hydrogels with optimal properties. Here we report the hydrogelation of peptide hydrogelators by an enzymatically induced pH switch, which involves the combination of glucose oxidase and catalase with D-glucose as the substrate, in which both the gelation kinetics and thermodynamics can be controlled by the concentrations of D-glucose. This novel hydrogelation method could result in hydrogels with higher mechanical stability and lower hydrogelation concentrations. We further illustrate the application of this hydrogelation method to differentiate different D-glucose levels.
基金
supported by the National Natural Science Foundation of China(Grant No.11304156)
the Priority Academic Program Development of Jiangsu Higher Education,Jiangsu PhD Gathering Scheme,the Technology Foundation for Selected Overseas Chinese Scholar,and the Scientific Research Foundationfor the Returned Overseas Chinese Scholars,State Education Ministry,China
