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

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 n...

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Bibliographic Details
Published inPeptide science (Hoboken, N.J.) Vol. 113; no. 1
Main Authors Bluntzer, Marie T. J., O'Connell, James, Baker, Terry S., Michel, Julien, Hulme, Alison N.
Format Journal Article
LanguageEnglish
Published Hoboken, USA John Wiley & Sons, Inc 01.01.2021
Subjects
analysis
crystal structure
design
stapled peptides
therapeutics
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Summary: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.
Bibliography:Funding information
Medical Research Scotland, Grant/Award Number: PhD‐1042‐2016; UCB Celltech
ISSN:2475-8817
2475-8817
DOI:10.1002/pep2.24191