(316d) Investigation of Polyproline II Peptides As Antifouling Biomaterials

Biomaterials derived from polyproline (PPII) peptide sequences offer significant promise due to their diverse applications, including as antifouling agents for biomaterials and as anchors that encourage high density of other peptide sequences. However, the precise mechanisms underlying their antifouling behavior is not fully understood. This study comprehensively investigates antifouling properties of PPII peptides using bovine serum albumin (BSA) as a model foulant while varying guest amino acids within the PPII sequence. By varying the sequence and controlling their adsoprtion, aim to investigate multiple properties, including secondary structure, hydrophobicity, rate constant of rearrangement, and surface coverage, to elucidate their impact on these on antifouling mechanisms. Our findings indicate that surface coverage and incorporation of proline in the sequence has a significant positive impact on antifouling properties. Moreover, this research marks the first exploration of human mesenchymal cells (hMSCs) as foulants on PPII-functionalized surfaces, revealing successful minimization of cell adhesion that correlates with the model foulant results. In conclusion, our research underscores the potential of PPII design and application as an antifouling biomaterial, paving the way for future advancements in this field including use of these sequences as way to control hMSC spreading and attachment.