Type I collagen prevents amyloid aggregation of hen egg white lysozyme

• Strong inhibition of HEW lysozyme amyloid aggregation by type I collagen.
• Type I collagen suppresses seeded amyloid aggregation of lysozyme.
• Substantial gain of conformational stability of lysozyme in the presence of collagen.
• Catalytic activity of lysozyme remains unaltered in the presence of collagen.
• Obtained results may have implications for collagen based therapeutics against amyloid linked diseases.

Both collagen and amyloidogenic proteins have an inherent ability to undergo a self-assembly process leading to formation of supramolecular structures. Though our understanding of collagen–amyloid link is very poor, a few experimental evidences have indicated the protective nature of collagen against amyloid fibril formation. To further our understanding of collagen–amyloid relationship, we have explored the role of type I collagen on amyloid-aggregation of lysozyme. Thioflavin-T assay data indicated strong inhibition of both spontaneous and seeded aggregation of lysozyme by collagen. Both chemical and thermal denaturation experiments have showed increased lysozyme stability in the presence of collagen. However, the presence of collagen did not alter lysozyme activity. These findings confirm that type I collagen is capable of blocking or interfering with the amyloid aggregation of lysozyme, and the results may have significant implications for the design of collagen based therapeutics against aggregation of disease linked amyloidogenic proteins.

Figure optionsDownload as PowerPoint slide