Design and synthesis of a tetracyclic tripeptide mimetic frozen in a polyproline type II (PP2) helix conformation-Reference-Cited by-同舟云学术

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Design and synthesis of a tetracyclic tripeptide mimetic frozen in a polyproline type II (PP2) helix conformation

Published:2022 Issue:47 Volume:20 Page:9368-9377
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Klein Marco T.¹,Krause Bernhard M.¹^ORCID,Neudörfl Jörg-Martin¹,Kühne Ronald²,Schmalz Hans-Günther¹^ORCID

Affiliation:

1. University of Cologne, Department of Chemistry, Greinstrasse 4, 50939 Köln, Germany

2. Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Strasse 10, 13125 Berlin, Germany

Abstract

The geometrically defined XPP tripeptide analogue ProM-19 was stereoselectively synthesized and converted into a potential EVH1 ligand by peptide synthesis.

Funder

Bundesministerium für Bildung und Forschung

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/OB/D2OB01857H

Reference50 articles.

1. Assessing Helical Protein Interfaces for Inhibitor Design

2. Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?

3. Targeting Protein-Protein Interactions with Small Molecules: Challenges and Perspectives for omputational Binding Epitope Detection and Ligand Finding

4. Interfacial inhibition of macromolecular interactions: nature's paradigm for drug discovery

5. Recognition of Proline-Rich Motifs by Protein-Protein-Interaction Domains

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