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

Nekkaa, Imane [Nekkaa, Imane (gyógyszerkémia), author] Department of Pharmaceutical Chemistry (USZ / FP); Bogdán, Dóra* [Bogdán, Dóra (Szerves kémia, gy...), author] Department of Organic Chemistry (SU / FP); Gáti, Tamás; Béni, Szabolcs [Béni, Szabolcs (NMR-spektroszkópi...), author] Department of Pharmacognosy (SU / FP); Juhász, Tünde [Juhász, Tünde (Enzimológia), author] Biomolecular Self-Assembly Research Group (MTA TTK / AKI); Palkó, Márta [Palkó, Márta (Gyógyszerkémia, s...), author] Department of Pharmaceutical Chemistry (USZ / FP); Paragi, Gábor [Paragi, Gábor (molekulafizika, m...), author] Department of Medical Chemistry (USZ / ÁOK); MTA-SZTE Biomimetic Systems Research Group (USZ / ÁOK / DMC); Tóth, Gábor K. [Tóth, Gábor (Peptidkémia), author] Department of Medical Chemistry (USZ / ÁOK); MTA-SZTE Biomimetic Systems Research Group (USZ / ÁOK / DMC); Fülöp, Ferenc ✉ [Fülöp, Ferenc (Kémia), author] Department of Pharmaceutical Chemistry (USZ / FP); Mándity, István M. ✉ [Mándity, István (Gyógyszerkémia, g...), author] Department of Organic Chemistry (SU / FP); Artificial Transporters Research Group (MTA TTK / AKI)

English Scientific Article (Journal Article)
Published: CHEMICAL COMMUNICATIONS 1359-7345 1364-548X 55 (21) pp. 3061-3064 2019
  • SJR Scopus - Ceramics and Composites: D1
Identifiers
Enantiodiscriminative helix formation was observed for beta-peptide H14 helices. This observation is caused by the synperiplanar orientation of H-O atoms which is more unfavorable than those for H-H interaction. The 1,2 H-O interaction leads to the destruction of the helical structure. The introduction of a double C-C bond in the backbone rules out helix formation.
Citation styles: IEEEACMAPAChicagoHarvardCSLCopyPrint
2020-08-08 23:11