Microwell plate-based absorption and fluorescence assays were developed to evaluate the quality and shelf life of peptide activation reagents in order to establish metrology during solid phase peptide synthesis, peptide couplings, and the building of peptide microarrays.

A novel antimicrobial peptide, referred to as Opisin, was discovered from the scorpion Opistophthalmus glabrifrons. Opisin possesses strong antimicrobial activity against antibiotics-resistant pathogens, such as methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococcus (VRE). This suggests that Opisin has great potential for the treatment of infections caused by MRSA and VRE.

The isothiocyanate reagents proved to selectively react with N-methoxyglycine residue introduced to the synthetic peptides. This reaction was successfully used for the site-specific fluorescent labeling of synthetic human β-defensin.

There was a rapid eradication of established two biofilms by short cinnamic–peptide hybrids within 6 h at microgram per millilitre concentrations and no significant toxicity was demonstrated. It is potential as future antimicrobial therapies to combat antimicrobial resistance.

Temporin-1Tl (TL) analogs possess improved anti-inflammatory activity and retain antimicrobial activity without a significant increase in hemolysis. TL analogs have considerable potential for future development as antimicrobial and anti-inflammatory agents.

This study concerns the functionalization of poly-ɛ-caprolactone or poly(l-lactic acid-co-ɛ-caprolactone) electrospun scaffolds with a photoreactive peptide containing four Gly-Arg-Gly-Asp-Ser-Pro motifs. Different peptide densities on the scaffold surface were obtained by simply modifying the peptide concentration used in the scaffold pretreatment before UV irradiation. The scaffolds functionalized enhance adhesion of human umbilical vein endothelial cells at 24 h with a dose-dependent effect.