This study provides a novel method for constructing an mRNA-displayed bicyclic peptide library cyclized through 1,3,5-tris(methyl)benzene by ribosomally incorporating N-acetyl-3,5-bis(chloromethyl)benzylthio-L-alanine.
TBMB linker containing bicyclic temporin L peptide with three cysteine residues. 3D structure of the bicyclic peptide and its interaction with the main protease of SARS-CoV-2.
This work presents an efficient mRNA display protocol for making large libraries of bicyclic peptides and evaluating their performance vs. linear and monocyclic formats for affinity, specificity & plasma stability in a selection against FGFR3c.
We report a sortase-based macrocyclization strategy in which low-reactive electrophiles are introduced into the SrtA recognition sequence (LPXTG) to enable the construction of phage-displayed peptide macrocycle libraries for ligand discovery.
Owing to their special spatial structures, peptide-based macrocycles have recently shown tremendous promise in multidisciplinary research ranging from potent antibiotics against resistant strains to functional biomaterials with novel properties.