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Issue 29, 2013
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Minimalistic amino amides as models to study N–H⋯π interactions and their implication in the side chain folding of pseudopeptidic molecules

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Abstract

The structural study of simple amino amides derived from natural amino acids showed a unique conformational pattern for the aromatic residues, being clearly different from that for the aliphatic derivatives. The results from a detailed NMR analysis, supported by DFT calculations, indicate that the aromatic side chain tends to fold over the amino amide moiety, involving a stabilizing polar N–H⋯π interaction. The implications of this folding in the establishing of non-covalent interactions is also discussed.

Graphical abstract: Minimalistic amino amides as models to study N–H⋯π interactions and their implication in the side chain folding of pseudopeptidic molecules

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Publication details

The article was received on 29 Jan 2013, accepted on 30 Apr 2013 and first published on 01 May 2013


Article type: Paper
DOI: 10.1039/C3RA41843J
Citation: RSC Adv., 2013,3, 11556-11565
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    Minimalistic amino amides as models to study N–H⋯π interactions and their implication in the side chain folding of pseudopeptidic molecules

    E. Faggi, S. V. Luis and I. Alfonso, RSC Adv., 2013, 3, 11556
    DOI: 10.1039/C3RA41843J

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