Toward predicting silver ion binding in proteins.

The binding of metal ions in proteins is often crucial for their function and hence for life. Silver is known to possess antimicrobial properties, yet little is known about the exact molecular mechanism of action. Based on the silver binding tetrapeptide moieties HXXM, and MXXH found in the silver efflux pump protein SilE, we studied the influence of the individual amino acids X and X and found trends that may be important in general metal ion binding in proteins.

Functionalization of hydrophobic surfaces with antimicrobial peptides immobilized on a bio-interfactant layer.

The design of functionalized polymer surfaces using bioactive compounds has grown rapidly over the past decade within many industries including biomedical, textile, microelectronics, bioprocessing and food packaging sectors. Polymer surfaces such as polystyrene (PS) must be treated using surface activation processes prior to the attachment of bioactive compounds. In this study, a new peptide immobilization strategy onto hydrocarbonaceus polymer surfaces is presented.