The 1,3‐diyne linker as a rigid “ i , i +7” staple for α‐helix stabilization: Stereochemistry at work-Reference-Cited by-同舟云学术

The 1,3‐diyne linker as a rigid “ i , i +7” staple for α‐helix stabilization: Stereochemistry at work

Published:2019-06-18 Issue:7 Volume:25 Page:
ISSN:1075-2617
Container-title:Journal of Peptide Science
language:en
Short-container-title:J Pep Sci

Author:

Verlinden Steven¹,Geudens Niels²,Van holsbeeck Kevin¹²,Mannes Morgane¹,Martins José C.²,Verniest Guido¹³,Ballet Steven¹^ORCID

Affiliation:

1. Research Group of Organic Chemistry, Department of Chemistry and Department of Bioengineering Sciences, Faculty of Sciences and Bioengineering SciencesVrije Universiteit Brussel Brussels Belgium

2. NMR and Structure Analysis Unit, Department of Organic and Macromolecular ChemistryGhent University Ghent Belgium

3. Predictive Analytics and Stability Sciences, Center of Excellence, CRS, Analytical Development, PDMS, DPDS, Janssen Research and DevelopmentJanssen Pharmaceutical Companies of Johnson & Johnson Beerse Belgium

Funder

Fonds Wetenschappelijk Onderzoek

Publisher

Wiley

Subject

Organic Chemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,General Medicine,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/psc.3194

Reference38 articles.

1. Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes

2. Modulating protein–protein interactions: the potential of peptides

3. Assessing Helical Protein Interfaces for Inhibitor Design

4. Small-molecule inhibitors of protein–protein interactions: progressing towards the dream

5. Inhibition of protein–protein interactions using designed molecules

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