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Design and Synthetic Strategies for Helical Peptides

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Cyclic Peptide Design

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2001))

Abstract

Abnormal protein–protein interactions (PPIs) are the basis of multiple diseases, and the large and shallow PPI interfaces make the target “undruggable” for traditional small molecules. Peptides, emerging as a new therapeutic modality, can efficiently mimic PPIs with their large scaffolds. Natural peptides are flexible and usually have poor serum stability and cell permeability, features that limit their further biological applications. To satisfy the clinical application of peptide inhibitors, many strategies have been developed to constrain peptides in their bioactive conformation. In this report, we describe several classic methods used to constrain peptides into a fixed secondary structure which could significantly improve their biophysical properties.

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Authors and Affiliations

  1. State Key Laboratory of Chemical Oncogenomics, Peking University, Shenzhen Graduate School, Peking, China

    Licheng Tu, Dongyuan Wang & Zigang Li

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  1. Licheng Tu
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  2. Dongyuan Wang
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  3. Zigang Li
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Corresponding author

Correspondence to Zigang Li .

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Editors and Affiliations

  1. Hit Discovery and Optimization, Pfizer R&D, Groton, CT, USA

    Gilles Goetz

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Tu, L., Wang, D., Li, Z. (2019). Design and Synthetic Strategies for Helical Peptides. In: Goetz, G. (eds) Cyclic Peptide Design. Methods in Molecular Biology, vol 2001. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9504-2_7

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  • DOI: https://doi.org/10.1007/978-1-4939-9504-2_7

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  • Publisher Name: Humana, New York, NY

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