Adhesion and phase behavior of adhesive peptides from biofilms

Adhesives that function in wet environments are widely used in ships, fishing industry, etc. Also, bio-adhesives are extensively used in biomedical applications where there is a need to adhere two wet surfaces. To search for better adhesive materials that function in an aqueous environment, engineers have extensively studied adhesive proteins from mussels and barnacles, leading to major insights into biological adhesion, often involving the formation of phase separated condensates. However, mussel foot proteins (mfps) are sensitive to environmental conditions including oxygen and pH, limiting their wide application. In a serendipitous discovery while studying how Vibrio cholerae biofilms adhere to surfaces, we discovered a short peptide sequence made of 57-amino acids that is majorly responsible for Vc adhesion to various abiotic surfaces. Abundant in lysine, tyrosine, tryptophane, and threonine, the sequence shares similarity with mfps but also important differences. In this talk, I am going to describe our recent progress in understanding how this unique sequence balances the tendency to LLPS and to adhere to surfaces in order to maximize its adhesive performance.