The Construction of a Genetically Encoded, Phage-Displayed Cyclic-Peptide Library. Chen, P. C. & Liu, W. R. In Hussein, W. M., Stephenson, R. J., & Toth, I., editors, Peptide Conjugation: Methods and Protocols, of Methods in Molecular Biology, pages 219–230. Springer US, New York, NY, 2021. ![The Construction of a Genetically Encoded, Phage-Displayed Cyclic-Peptide Library [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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 Nε-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.
@incollection{chen_construction_2021,
address = {New York, NY},
series = {Methods in {Molecular} {Biology}},
title = {The {Construction} of a {Genetically} {Encoded}, {Phage}-{Displayed} {Cyclic}-{Peptide} {Library}},
isbn = {978-1-07-161617-8},
url = {https://doi.org/10.1007/978-1-0716-1617-8_17},
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 Nε-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.},
language = {en},
urldate = {2021-11-24},
booktitle = {Peptide {Conjugation}: {Methods} and {Protocols}},
publisher = {Springer US},
author = {Chen, Peng-Hsun Chase and Liu, Wenshe Ray},
editor = {Hussein, Waleed M. and Stephenson, Rachel J. and Toth, Istvan},
year = {2021},
doi = {10.1007/978-1-0716-1617-8_17},
keywords = {Cyclic peptides, HDAC8, Nε-acryloyl-lysine, Phage display, Proximity-driven cyclization},
pages = {219--230},
}
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