The Construction of a Genetically Encoded, Phage-Displayed Cyclic-Peptide Library. Chapter

abstract

• Due to the great potentials of cyclic peptides as therapeutic agents, several phage-displayed peptide libraries in which cyclization is achieved by the covalent linkage of cysteines have been previously demonstrated to identify cyclic-peptide ligands for therapeutic targets. While problems remain in these cysteine conjugation strategies, we have invented a phage display technique in which its displayed peptides are cyclized through a proximity-driven Michael addition reaction between a cysteine and an amber-codon-encoded N-acryloyl-lysine (AcrK). Using a randomized 6-mer library in which peptides were cyclized at two ends through a cysteine-AcrK linker, we demonstrated the successful selection of a potent ligand, CycH8a, for histone deacetylase 8 (HDAC8). We believe this approach will find broad applications in drug discovery.

authors

• Liu, Wenshe

author list (cited authors)

• Chen, P., & Liu, W. R.

citation count

• 1

complete list of authors

• Chen, Peng-Hsun Chase||Liu, Wenshe Ray

Book Title

• Peptide Conjugation

publication date

• January 2021

publisher

• Springer Nature  Publisher

published in

• Methods in molecular biology (Clifton, N.J.)  Journal

keywords

• Bacteriophages
• Cyclic Peptides
• Cysteine
• Hdac8
• Ligands
• Nε-acryloyl-lysine
• Peptide Library
• Peptides
• Peptides, Cyclic
• Phage Display
• Proximity-driven Cyclization

PubMed Central ID

• 34386961

Digital Object Identifier (DOI)

• 10.1007/978-1-0716-1617-8_17

International Standard Book Number (ISBN) 13

• 9781071616161

start page

• 219

end page

• 230

volume

• 2355

URL

• http://dx.doi.org/10.1007/978-1-0716-1617-8_17