• Odegrip et al. (2004) PNAS, 101, 2806–2810

• Eldridge et al. (2009) PEDS, 22, 691–698

Affinity and specificity

• A low nM inhibitor of a protein that was isolated from a naïve 16-mer library.  The protein was crystallised with the inhibitor  bound. Several different peptides overlapped the same site.
• Peptides have been isolated to thrombin and HIV-1 gp41. Maturation has led to these having subnanomolar affinities. Both are less than 25 amino acids.

Stability

• An inhibitor with low nM IC₅₀ selected from a naive 18-mer library. This had high selectivity over other isoforms of the protein. Different activation pathways inhibited with different affinities.
• Peptides have been isolated that inhibit NGF binding to its receptor. These have low nM IC₅₀s in competition assays and prevent a phenotypic change in cells.

Biological activity

• A natural GPCR ligand was subjected to maturation for stability. Peptides were isolated that maintained activity but had greater stability in plasma.
• A natural antimicrobial peptide was matured for stability. Peptides were more stable and had greater activity.