N-Difluoromethyl-triazole as a constrained scaffold in peptidomimetics-Reference-Cited by-同舟云学术

N-Difluoromethyl-triazole as a constrained scaffold in peptidomimetics

Published:2017 Issue:36 Volume:53 Page:5024-5027
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Mamone M.¹²³⁴⁵,Gonçalves R. S. B.⁶⁷⁸⁹¹⁰,Blanchard F.¹¹¹²¹³¹⁴¹⁵,Bernadat G.¹²³⁴⁵,Ongeri S.¹²³⁴⁵^ORCID,Milcent T.¹²³⁴⁵^ORCID,Crousse B.¹²³⁴⁵^ORCID

Affiliation:

1. Univ Paris-Sud

2. BioCIS

3. CNRS

4. Faculté de Pharmacie

5. 92290 Châtenay-Malabry

6. Departamento de Química Orgânica

7. Instituto de Química

8. Universidade Federal do Rio de Janeiro

9. Rio de Janeiro

10. Brazil

11. Institut de Chimie des Substances Naturelles

12. CNRS UPR 2301

13. Univ. Paris-Sud

14. Université Paris-Saclay

15. 91198 Gif-sur-Yvette

Abstract

The N-difluoromethyl triazolo-β-aza-ε-amino acid present in the core of peptides led to constrained conformations due to CH–F and NH–F interactions.

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2017/CC/C7CC01298E

Reference47 articles.

1. Peptidomimetics and the template approach to nucleation of β-sheets and α-helices in peptides

2. Medicinal Chemistry in the Golden Age of Biology: Lessons from Steroid and Peptide Research

3. Templates That Induce .alpha.-Helical, .beta.-Sheet, and Loop Conformations

4. Comprehensive Peptidomimetic Libraries Targeting Protein–Protein Interactions

5. The growing applications of click chemistry

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