A set of pairs of parallel coiled-coil-forming peptides was designed and tested. The design based on maximizing the difference in stability between the desired pairs and the most stable unwanted pairs. We used N-terminal helix-initiator residues, favorable combinations of electrostatic and hydrophobic interactions, and a negative design based on burial of Asn residues. The 36 pair combinations of the eight peptides were analysed by CD. Each peptide formed a high level of alpha-helical structure exclusively in combination with its designed partner confirming the orthogonality of peptide pairs.
COBISS.SI-ID: 4534810
We studied the possibility of surface functionalization with bioactive peptides for application in medicine. The model substrate was surface coated to enable binding of the model peptide with antimicrobial activity. The surface obtained in such a way exhibited biocidic activity and reduced the concentration of the Gram-negative bacterium Escherichia coli for more than five orders of magnitude. Surface coatings with antimicrobial activity are applicable in medical devices, such as catheters and implants, for prevention of microbial biofilm formation, which causes severe infections.
COBISS.SI-ID: 4471578