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Cited by 186

The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.

Cyclic and Macrocyclic Peptides as Chemical Tools To Recognise Protein Surfaces and Probe Protein–Protein Interactions

Open access
Cardote, Teresa A. F., Ciulli, Alessio·2016·ChemMedChem

Abstract

Targeting protein surfaces and protein–protein interactions (PPIs) with small molecules is a frontier goal of chemical biology and provides attractive therapeutic opportunities in drug discovery. The molecular properties of protein surfaces, including their shallow features and lack of deep binding pockets, pose significant challenges, and as a result have proved difficult to target. Peptides are ideal candidates for this mission due to their ability to closely mimic many structural features of protein interfaces. However, their inherently low intracellular stability and permeability and high in vivo clearance have thus far limited their biological applications. One way to improve these properties is to constrain the secondary structure of linear peptides by cyclisation. Herein we review various classes of cyclic and macrocyclic peptides as chemical probes of protein surfaces and modulators of PPIs. The growing interest in this area and recent advances provide evidence of the potential of developing peptide‐like molecules that specifically target these interactions.

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Metadata

Authors
Cardote, T. A. F., & Ciulli, A.
Venue
ChemMedChem
Publisher
Wiley
Published
2015-11-13
Volume
11
Issue
8
Pages
787-794
ISSN
  • 1860-7179 (ISSN-L)
  • 1860-7187
OpenAlex
W2101040826
Cited by
186
References
11
FWCI
6.82
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Cyclic and Macrocyclic Peptides as Chemical Tools To Recognise Protein Surfaces and Probe Protein–Protein Interactions. https://app.cochat.ai/papers/10.1002/cmdc.201500450
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Cardote, T. A. F., & Ciulli, A. (2016). Cyclic and Macrocyclic Peptides as Chemical Tools To Recognise Protein Surfaces and Probe Protein–Protein Interactions. ChemMedChem. https://doi.org/10.1002/cmdc.201500450

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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