SM04.03.03 : Effects of Antifouling Performance with Rational Sequencing of Amino Acids Within a Peptide Chain

5:00 PM–7:00 PM Apr 3, 2018 (America - Denver)

PCC North, 300 Level, Exhibit Hall C-E

Sheng Long Gaw1 Nir Sivan2 Gowripriya Sakala2 Zhichuan Jason Xu1 Pooi See Lee1 Meital Reches2

1, Nanyang Technological University, Singapore, , Singapore
2, The Hebrew University of Jerusalem, Jerusalem, , Israel

Amphiphilic coating has gained much attention due to its dual hydrophobic and hydrophilic properties. Due to their bifunctional nature, it has been suggested that the amphiphilic coatings resist the attachment of organisms and the adhesion of complex protein or glycoprotein adhesives secreted by the colonizing organisms. Most amphiphilic coatings are polymers based on oligo- and polyethylene glycols (OEG and PEG). Spontaneous self-assembled amphiphilic peptide brings advantages of the protease resistance property of the backbone sequencing, precise control of molecular weight and side chain composition versatility. In this work, we focus on the antifouling performance of a self-assembly amphiphilic tripeptide with rational positioning of the amino acids within the peptide chain and influence of the C and N terminus when the amino acids are in the same position. We have selected 3, 4-dihydroxy-L-phenylalanine (DOPA) as the binding amino acid to the surface, 4-fluoro-phenylalanine (Phe(4F)) as the hydrophobic amino acid due to its fluorinated side chain, and Lysine (Lys) as the hydrophilic amino acids. Our result indicates that the sequencing of amino acids affects the antifouling performance, particularly with lysine adjacent to a DOPA at the C terminal and Phe(4F) at the N terminal.