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Genetically encoded cyclic peptide libraries: From hit to lead and beyond

Genetically encoded cyclic peptide libraries: From hit to lead and beyond
Genetically encoded cyclic peptide libraries: From hit to lead and beyond

With the increasing utilization of high-throughput screening for lead identification in drug discovery, the need for easily constructed and diverse libraries which cover significant chemical space is greater than ever. Cyclic peptides address this need; they combine the advantageous properties of peptides (ease of production, high diversity, high potential specificity) with increased resistance to proteolysis and often increased biological activity (due to conformational locking). There are a number of techniques for the generation and screening of cyclic peptide libraries. As drug discovery moves toward tackling challenging targets, such as protein–protein interactions, cyclic peptide libraries are expected to continue producing hits where small molecule libraries may be stymied. However, it is important to design robust systems for the generation and screening of these large libraries, and to be able to make sense of structure–activity relationships in these highly variable scaffolds. There are a plethora of possible modifications that can be made to cyclic peptides, which is both a weakness and a strength of these scaffolds; high variability will allow more precise tuning of leads to targets, but exploring the whole range of modifications may become an overwhelming challenge.

Cyclic peptides, Hit to lead, mRNA display, Protein–protein interaction inhibitors, SICLOPPS
0076-6879
117-134
Academic Press
Valentine, Jacob
c5554f03-85d6-492c-b025-d47d83501e9d
Tavassoli, Ali
d561cf8f-2669-46b5-b6e1-2016c85d63b2
Lesburg, Charles A.
Valentine, Jacob
c5554f03-85d6-492c-b025-d47d83501e9d
Tavassoli, Ali
d561cf8f-2669-46b5-b6e1-2016c85d63b2
Lesburg, Charles A.

Valentine, Jacob and Tavassoli, Ali (2018) Genetically encoded cyclic peptide libraries: From hit to lead and beyond. In, Lesburg, Charles A. (ed.) Methods in Enzymology. (Methods in Enzymology, , (doi:10.1016/bs.mie.2018.09.020), 610) Academic Press, pp. 117-134. (doi:10.1016/bs.mie.2018.09.020).

Record type: Book Section

Abstract

With the increasing utilization of high-throughput screening for lead identification in drug discovery, the need for easily constructed and diverse libraries which cover significant chemical space is greater than ever. Cyclic peptides address this need; they combine the advantageous properties of peptides (ease of production, high diversity, high potential specificity) with increased resistance to proteolysis and often increased biological activity (due to conformational locking). There are a number of techniques for the generation and screening of cyclic peptide libraries. As drug discovery moves toward tackling challenging targets, such as protein–protein interactions, cyclic peptide libraries are expected to continue producing hits where small molecule libraries may be stymied. However, it is important to design robust systems for the generation and screening of these large libraries, and to be able to make sense of structure–activity relationships in these highly variable scaffolds. There are a plethora of possible modifications that can be made to cyclic peptides, which is both a weakness and a strength of these scaffolds; high variability will allow more precise tuning of leads to targets, but exploring the whole range of modifications may become an overwhelming challenge.

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More information

e-pub ahead of print date: 24 October 2018
Published date: 2018
Keywords: Cyclic peptides, Hit to lead, mRNA display, Protein–protein interaction inhibitors, SICLOPPS

Identifiers

Local EPrints ID: 425966
URI: http://eprints.soton.ac.uk/id/eprint/425966
ISSN: 0076-6879
PURE UUID: d147b55e-c5e2-406a-bb87-7bc18c9b63fb
ORCID for Ali Tavassoli: ORCID iD orcid.org/0000-0002-7420-5063

Catalogue record

Date deposited: 08 Nov 2018 17:30
Last modified: 15 Sep 2021 01:51

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Contributors

Author: Jacob Valentine
Author: Ali Tavassoli ORCID iD
Editor: Charles A. Lesburg

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