Substrate mimetics are excellent tools for protease‐mediated peptide synthesis that enable
the coupling of peptides independently of the primary specificity of the enzyme without …

Although proteases are capable of synthesizing peptide bonds via the reverse of proteolysis,
they are not proficient at peptide fragment ligation. Further manipulations are needed to shift …

Two main drawbacks seriously restrict the synthetic value of proteases as reagents in
peptide fragment coupling:(i) native proteolytic activity and, thus, risk of undesired peptide …

Selective incorporation of non-natural amino acid residues into proteins is a powerful
approach to delineate structure–function relationships. Although many methodologies are …

This article reviews the latest developments in protease-catalyzed peptide synthesis
focusing on the use of substrate mimetics. The substrate mimetics approach takes …

This article reports on the design and characteristics of substrate mimetics in protease-
catalyzed reactions. Firstly, the basis of protease-catalyzed peptide synthesis and the …

The substrate mimetics approach is a versatile method for small‐scale enzymatic peptide‐
bond synthesis in aqueous systems. The protease‐recognized amino acid side chain is …

Chymotrypsin family serine proteases play essential roles in key biological and pathological
processes and are frequently targets of drug discovery efforts. This large enzyme family is …

Identification of substrate-analog trypsin inhibitors through the screening of synthetic
peptide combinatorial libraries Page 1 Biochemistry 1993, 32, 11035-11041 11035 …

Achromobacter protease I (API), a lysine-specific serine-protease of the trypsin family, has
an aromatic-ring stacking Trp 169-His 210 in close proximity to the reactive site. In order to …