Designing stapled peptides to inhibit protein-protein interactions: An analysis of successes in a rapidly changing field

Marie T.J. Bluntzer; James O'Connell; Terry S. Baker; Julien Michel; Alison N. Hulme

doi:10.1002/pep2.24191

Designing stapled peptides to inhibit protein-protein interactions: An analysis of successes in a rapidly changing field

Marie T.J. Bluntzer, James O'Connell, Terry S. Baker, Julien Michel, Alison N. Hulme^*

^*Corresponding author for this work

Research output: Contribution to journal › Review article › peer-review

Abstract / Description of output

Two decades after their discovery, stapled peptide methodologies have evolved to a point where they can be used with confidence to generate therapeutic leads. Research groups across the world are testing innovative methodologies for their design, with dozens of publications released every month. A number of stapled peptide drug candidates have recently entered clinical trials. In this review, we provide an overview of successful methods for their construction, highlight trends in the deposited crystal structures of stapled peptide complexed to their targets and discuss properties that contribute towards improved pharmacological profiles.

Original language	English
Journal	Peptide Science
Early online date	12 Oct 2020
DOIs	https://doi.org/10.1002/pep2.24191
Publication status	E-pub ahead of print - 12 Oct 2020

Keywords / Materials (for Non-textual outputs)

analysis
crystal structure
design
stapled peptides
therapeutics

Access to Document

10.1002/pep2.24191

20201029_Hulme_pep2.24191Final published version, 6.02 MBLicence: Creative Commons: Attribution Non-Commercial (CC-BY-NC)

https://onlinelibrary.wiley.com/doi/full/10.1002/pep2.24191

Cite this

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title = "Designing stapled peptides to inhibit protein-protein interactions: An analysis of successes in a rapidly changing field",

abstract = "Two decades after their discovery, stapled peptide methodologies have evolved to a point where they can be used with confidence to generate therapeutic leads. Research groups across the world are testing innovative methodologies for their design, with dozens of publications released every month. A number of stapled peptide drug candidates have recently entered clinical trials. In this review, we provide an overview of successful methods for their construction, highlight trends in the deposited crystal structures of stapled peptide complexed to their targets and discuss properties that contribute towards improved pharmacological profiles.",

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author = "Bluntzer, {Marie T.J.} and James O'Connell and Baker, {Terry S.} and Julien Michel and Hulme, {Alison N.}",

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AU - Bluntzer, Marie T.J.

AU - O'Connell, James

AU - Baker, Terry S.

AU - Michel, Julien

AU - Hulme, Alison N.

PY - 2020/10/12

Y1 - 2020/10/12

N2 - Two decades after their discovery, stapled peptide methodologies have evolved to a point where they can be used with confidence to generate therapeutic leads. Research groups across the world are testing innovative methodologies for their design, with dozens of publications released every month. A number of stapled peptide drug candidates have recently entered clinical trials. In this review, we provide an overview of successful methods for their construction, highlight trends in the deposited crystal structures of stapled peptide complexed to their targets and discuss properties that contribute towards improved pharmacological profiles.

AB - Two decades after their discovery, stapled peptide methodologies have evolved to a point where they can be used with confidence to generate therapeutic leads. Research groups across the world are testing innovative methodologies for their design, with dozens of publications released every month. A number of stapled peptide drug candidates have recently entered clinical trials. In this review, we provide an overview of successful methods for their construction, highlight trends in the deposited crystal structures of stapled peptide complexed to their targets and discuss properties that contribute towards improved pharmacological profiles.

KW - analysis

KW - crystal structure

KW - design

KW - stapled peptides

KW - therapeutics

U2 - 10.1002/pep2.24191

DO - 10.1002/pep2.24191

M3 - Review article

AN - SCOPUS:85092369885

SN - 2475-8817

JO - Peptide Science

JF - Peptide Science

ER -

Designing stapled peptides to inhibit protein-protein interactions: An analysis of successes in a rapidly changing field

Abstract / Description of output

Keywords / Materials (for Non-textual outputs)

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