Novel protein photocrosslinking and cryopolymerization method for cryogel-based antibacterial material synthesis

Abstract

Lysozyme (Lys), also known as muramidase or N-acetylmuramide glycanhydrolase, is a family of enzymes that damage bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. In this study, Lys was enhanced with a photosensitive facility by ruthenium chelate based monomers with a photosensitization and conjugation approach [amino acid (monomer) decorated and light underpinning conjugation approach]. Then, photosensitive Lys was allowed to interact with methacryloyl amido tyrosine (MATyr) monomer, which included tyrosine parts in its structure similar to those in the Lys structure. Two different types of cryogels including LysMATyr in their macropores were synthesized, LysMATyr cryogel and LysMATyrclay cryogel. These two materials were used for the measurement of the antibacterial activity on Gram-positive and Gram-negative bacteria. The effects of the modified Lys on Staphylococcus aureus and Micrococcus luteus were determined with a dilution plate method. The effects on Escherichia coli and S. aureus were determined with a turbidity method. According to the data, the LysMATyrclay modified embedded cryogel was effective on Gram-positive bacteria, and the LysMATyr modified embedded cryogel was so effective on Gram-negative bacteria