Literature DB >> 29809294

Environmental Effects Determine the Structure of Potential β-Amino Acid Based Foldamers.

Fredy Sussman1, Víctor M Sánchez-Pedregal1, Juan C Estévez1, Rosalino Balo1, Jesús Jiménez-Barbero2,3,4, Ana Ardá2, Ana Gimeno2, Miriam Royo5,6, M Carmen Villaverde1, Ramón J Estévez1.   

Abstract

This work shows that hybrid peptides formed by alternating trans-2-aminocyclopentanecarboxylic acid (trans-ACPC) and trans-2-aminocyclohexanecarboxylic acid (trans-ACHC) do not fold in the solvents typically used in the study of their homo-oligomers. Only when the peptides are assayed in SDS micelles are the predicted helical structures obtained. This indicates that the environment could play an equally important role (as the backbone stereochemistry) in determining their fold, possibly by providing a sequestered environment.
© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Entities:  

Keywords:  NMR spectroscopy; environmental effects; foldamers; micelles; molecular dynamics

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Year:  2018        PMID: 29809294     DOI: 10.1002/chem.201801953

Source DB:  PubMed          Journal:  Chemistry        ISSN: 0947-6539            Impact factor:   5.236


  1 in total

1.  Polyhydroxylated Cyclopentane β-Amino Acids Derived from d-Mannose and d-Galactose: Synthesis and Protocol for Incorporation into Peptides.

Authors:  Fernando Fernández; Alberto G Fernández; Rosalino Balo; Víctor M Sánchez-Pedregal; Miriam Royo; Raquel G Soengas; Ramón J Estévez; Juan C Estévez
Journal:  ACS Omega       Date:  2022-01-04
  1 in total

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