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This paper reports the rational design and synthesis of a beta-lactam conjugate. Treating the conjugate with beta-lactamase cleaves the scissile -lactam amide bond, releases a hydrogelator, and results in enzymatic formation of a supramolecular hydrogel. The process involves the use of a bacterial enzyme-the one causes antibiotic inactivation and accounts for resistance to beta-lactams in many clinical important pathogens-to catalyze the formation of the hydrogel. It offers an opportunity to investigate the kinetics of these types of enzymatic reactions, screen inhibitors of the enzyme, and provides a new candidate to generate hydrogels for biomedical applications.

This paper reports the rational design and synthesis of a beta-lactam conjugate. Treating the conjugate with beta-lactamase cleaves the scissile -lactam amide bond, releases a hydrogelator, and results in enzymatic formation of a supramolecular hydrogel. The process involves the use of a bacterial enzyme-the one causes antibiotic inactivation and accounts for resistance to beta-lactams in many clinical important pathogens-to catalyze the formation of the hydrogel. It offers an opportunity to investigate the kinetics of these types of enzymatic reactions, screen inhibitors of the enzyme, and provides a new candidate to generate hydrogels for biomedical applications.

This paper reports the rational design and synthesis of a beta-lactam conjugate. Treating the conjugate with beta-lactamase cleaves the scissile -lactam amide bond, releases a hydrogelator, and results in enzymatic formation of a supramolecular hydrogel. The process involves the use of a bacterial enzyme-the one causes antibiotic inactivation and accounts for resistance to beta-lactams in many clinical important pathogens-to catalyze the formation of the hydrogel. It offers an opportunity to investigate the kinetics of these types of enzymatic reactions, screen inhibitors of the enzyme, and provides a new candidate to generate hydrogels for biomedical applications.