Elusive π-helical peptide foldamers spotted by chiroptical studies-Reference-Cited by-同舟云学术

Elusive π-helical peptide foldamers spotted by chiroptical studies

Published:2020 Issue:5 Volume:18 Page:865-877
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Di Silvio Sergio¹²³⁴,Bologna Fabio¹²³⁴^ORCID,Milli Lorenzo¹²³⁴,Giuri Demetra¹²³⁴,Zanna Nicola¹²³⁴,Castellucci Nicola¹²³⁴,Monari Magda¹²³⁴^ORCID,Calvaresi Matteo¹²³⁴^ORCID,Górecki Marcin⁵⁶⁷⁴⁸^ORCID,Angelici Gaetano⁵⁶⁷⁴^ORCID,Tomasini Claudia¹²³⁴^ORCID,Pescitelli Gennaro⁵⁶⁷⁴^ORCID

Affiliation:

1. Dipartimento di Chimica “Giacomo Ciamician”

2. Alma Mater Studiorum Università di Bologna

3. 40126 Bologna

4. Italy

5. Dipartimento di Chimica e Chimica Industriale

6. Università di Pisa

7. 56124 Pisa

8. Institute of Organic Chemistry

Abstract

A series of oligomers containing alternate l-Ala and pGlu (pyroglutamic acid) both in the L and D form have been prepared and conformationally investigated by X-ray, NMR, UV/ECD, IR/VCD and molecular modelling.

Funder

Ministero dell’Istruzione, dell’Università e della Ricerca

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/OB/C9OB02313E

Reference72 articles.

1. Residue Requirements for Helical Folding in Short α/β-Peptides: Crystallographic Characterization of the 11-Helix in an Optimized Sequence

2. The complete chirospectroscopic signature of the peptide 310-helix in aqueous solution

3. Distinctive Circular Dichroism Signature for 14-Helix-Bundle Formation by β-Peptides