Polyproline peptide sequences have gained popularity as anchors for peptide-based self-assembled monolayers (SAMs) due to their attractive properties. In this work, peptides containing the polyproline II helix (PPII) conformation were designed and assembled on gold (Au). A quartz crystal microbalance with dissipation was used to characterize SAM formation kinetics and related properties. Peptides were designed with the sequence (GPPPPPG) 2 C. It was discovered that a biexponential adsorption and rearrangement model describes the binding kinetics of the PPII-containing peptide on Au. In this model, an initial reversible binding step is followed by an irreversible rearrangement step, given by parameter k t . This study found k t to be approximately 0.00064 s −1 for the PPII-containing peptides. Similarly, we found that the adsorption of the PPII-containing peptide on Au, given by ΔG ads , was thermodynamically favorable (−7.8 kcal mol −1 ) and comparable to other common thiol terminated SAMs on Au. Furthermore, we characterized SAM properties via QCM-D, Fouriertransform infrared (FTIR) spectroscopy, and electrochemical techniques to reveal high molecular density SAMs consisting of PPII helices. In addition, these SAMs were found to have high antifouling properties. Overall, this study characterizes the fundamental assembly mechanisms, particularly, rearrangement of PPII-containing peptides for the first time, which will be useful in the designing of future peptide-based SAMs with high surface coverage and antifouling properties.

Platinum-binding peptides have been used for fabrication of complex platinum nanomaterials such as catalysts, metallopharmaceuticals, and electrodes. In this review, we present understanding of the mechanisms behind platinum-binding (Pt-binding) peptides and the applications of the peptides as multifunctional biomaterials. We discuss how the surface recognition, the roles of individual amino acids, and arrangement of amino acid sequences interplay. Our summary on the current state of understanding of Pt-binding peptides highlights opportunities for interdisciplinary research which will expand the applicability of these multifunctional Pt-binding peptides.

Ever since the first observation of antagonism by microorganisms by Ernest Duchesne (E. Duchesne, Contribution à l’étude de la concurrence vitale chez les microorganisms. Antagonism entre les moisissures et les microbes, These pour obtenir le grade de docteur en medicine, Lyon, France, 1897), many scientists successfully identified and applied bacteriogenic bioactive compounds from soils to cure infection.