Flow-chemistry enabled efficient synthesis of β-peptides: backbone topology vs. helix formation-Reference-Cited by-同舟云学术

Flow-chemistry enabled efficient synthesis of β-peptides: backbone topology vs. helix formation

Published:2019 Issue:21 Volume:55 Page:3061-3064
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Nekkaa Imane¹²³⁴,Bogdán Dóra⁵⁶⁷⁸⁴,Gáti Tamás⁵⁶⁷⁸⁴,Béni Szabolcs⁹⁶⁷¹⁰⁴^ORCID,Juhász Tünde¹¹¹²¹³¹⁴⁴,Palkó Márta¹²³⁴,Paragi Gábor¹⁵²³⁴¹⁶,Tóth Gábor K.¹⁵²³⁴¹⁶,Fülöp Ferenc¹²³⁴,Mándity István M.¹²³⁴⁵^ORCID

Affiliation:

1. Institute of Pharmaceutical Chemistry

2. University of Szeged

3. H-6720 Szeged

4. Hungary

5. Department of Organic Chemistry

6. Faculty of Pharmacy

7. Semmelweis University

8. H-1092 Budapest

9. Department of Pharmacognosy

10. H-1085 Budapest

11. Institute of Materials and Environmental Chemistry

12. Research Center for Natural Sciences

13. Hungarian Academy of Sciences

14. H-1117 Budapest

15. Department of Medical Chemistry

16. MTA SZTE Biomimetic Systems Research Group

Abstract

Enantiodiscriminative helix formation was observed for β-peptide H14 helices when enantiomers of bridged bicyclic residues were introduced.

Funder

Nemzeti Kutatási és Technológiai Hivatal

Magyar Tudományos Akadémia

Országos Tudományos Kutatási Alapprogramok

Emberi Eroforrások Minisztériuma

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/2019/CC/C8CC10147G

Reference53 articles.

1. Foldamers: A Manifesto

2. A Field Guide to Foldamers

3. Peptidomimetic therapeutics: scientific approaches and opportunities

4. The World ofβ- andγ-Peptides Comprised of Homologated Proteinogenic Amino Acids and Other Components

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