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Constraining Peptide Conformations with the Help of Ring-Closing Metathesis
- Source :
- Synlett, 26(1), 1-5. Georg Thieme Verlag, Glas, A & Grossmann, T N 2015, ' Constraining Peptide Conformations with the Help of Ring-Closing Metathesis ', Synlett, vol. 26, no. 1, pp. 1-5 . https://doi.org/10.1055/s-0034-1379425
- Publication Year :
- 2015
- Publisher :
- Georg Thieme Verlag, 2015.
-
Abstract
- Chemical modifications are used to stabilize bioactive conformations of peptides thereby increasing their target affinity and selectivity. Such modified peptides proved particularly useful as inhibitors of protein–protein interactions. Most of these strategies aim at the stabilization of α-helices and β-sheets. The use of peptides with irregular secondary structure is hampered by a lack of appropriate stabilization approaches. Herein, we highlight a recent contribution from our group that uses ring-closing metathesis for the macrocyclization of peptides with irregular secondary structure. The peptide precursors are cyclized on solid support to provide cross-linked architectures that bind the ­human protein 14-3-3 thereby inhibiting its interaction with virulence factor exoenzyme S from Pseudomonas aeruginosa.
- Subjects :
- chemistry.chemical_classification
Stereochemistry
Organic Chemistry
protein-protein interactions
hydrophobic cross-links
Peptide
cyclic peptides
Metathesis
ring-closing metathesis
Cyclic peptide
Protein–protein interaction
Exoenzyme S
Ring-closing metathesis
chemistry
Pseudomonas aeruginosa
Protein secondary structure
Subjects
Details
- Language :
- English
- ISSN :
- 09365214
- Volume :
- 26
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Synlett
- Accession number :
- edsair.doi.dedup.....4c7c6ccac3648f22efc122b2d8454db6
- Full Text :
- https://doi.org/10.1055/s-0034-1379425