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1.
Org Biomol Chem ; 13(10): 3064-9, 2015 Mar 14.
Artigo em Inglês | MEDLINE | ID: mdl-25624112

RESUMO

This communication depicts an intriguing example of hydrogen-bonding reversal upon introduction of a sulfonamide linkage at the N-terminus of a synthetic reverse-turn peptide motif. The ready availability of two sulfonyl oxygen atoms, as hydrogen-bonding acceptors, combined with the inherent twisted conformation of sulfonamides are seen to act as switches that engage/disengage the hydrogen-bond at the sticky ends/termini.


Assuntos
Ligação de Hidrogênio , Enxofre/química , Motivos de Aminoácidos , Cristalografia por Raios X , Dimetil Sulfóxido/química , Espectroscopia de Ressonância Magnética , Modelos Moleculares , Estrutura Molecular , Oxigênio/química , Peptídeos/química , Polímeros/química , Estrutura Terciária de Proteína , Sulfonamidas/química , Temperatura
2.
Org Biomol Chem ; 11(41): 7072-5, 2013 Nov 07.
Artigo em Inglês | MEDLINE | ID: mdl-24057152

RESUMO

This communication describes the folding propensity of a heterofoldamer motif featuring proline (Pro) and anthranilic acid (Ant) residues in a 1:2:1 (α:ß:α) constitutional ratio. Structural investigations unequivocally suggest that the hydrogen-bonding network of this foldamer motif can be switched between 9-membered and 6-membered by modulating the backbone chirality and constitutional ratio of the amino acid residues.


Assuntos
Prolina/química , ortoaminobenzoatos/química , Ligação de Hidrogênio , Modelos Moleculares , Estrutura Molecular
3.
Org Biomol Chem ; 11(48): 8348-56, 2013 Dec 28.
Artigo em Inglês | MEDLINE | ID: mdl-24166475

RESUMO

Although known for their inferiority as hydrogen-bonding acceptors when compared to amides, esters are often found at the C-terminus of peptides and synthetic oligomers (foldamers), presumably due to the synthetic readiness with which they are obtained using protected peptide coupling, deploying amino acid esters at the C-terminus. When the H-bonding interactions deviate from regularity at the termini, peptide chains tend to "fray apart". However, the individual contributions of C-terminal esters in causing peptide chain end-fraying goes often unnoticed, particularly due to diverse competing effects emanating from large peptide chains. Herein, we describe a striking case of a comparison of the individual contributions of C-terminal ester vs. amide carbonyl as a H-bonding acceptor in the folding of a peptide. A simple two-residue peptide fold has been used as a testing case to demonstrate that amide carbonyl is far superior to ester carbonyl in promoting peptide folding, alienating end-fraying. This finding would have a bearing on the fundamental understanding of the individual contributions of stabilizing/destabilizing non-covalent interactions in peptide folding.


Assuntos
Amidas/química , Ésteres/química , Peptídeos/química , Dobramento de Proteína , Cristalografia por Raios X , Ligação de Hidrogênio , Modelos Moleculares , Estrutura Secundária de Proteína
4.
Org Biomol Chem ; 9(2): 367-9, 2011 Jan 21.
Artigo em Inglês | MEDLINE | ID: mdl-21082121

RESUMO

This communication describes the development of conformationally constrained unnatural aromatic amino acids, constructed on rigid backbone wherein the carboxyl and amino groups project in two dimensions (planes) on the aromatic framework. Such a feature offers the possibility of design and development of conformationally ordered synthetic oligomers with intriguing structural architectures distinct from those classically observed. Furthermore, such amino acids will have the potential to extend the conformational space available for foldamer design with diverse backbone conformation and structural architectures.


Assuntos
Aminoácidos Aromáticos/química , Cristalografia por Raios X , Modelos Moleculares , Conformação Molecular
5.
Org Biomol Chem ; 9(16): 5762-5, 2011 Aug 21.
Artigo em Inglês | MEDLINE | ID: mdl-21720634

RESUMO

This article describes a model peptide that concurrently displays both α- and ß-turns, as demonstrated by structural investigations using single crystal X-ray crystallography and solution-state NMR studies. The motif reported herein has the potential for the design of novel conformationally ordered synthetic oligomers with structural architectures distinct from those classically observed.


Assuntos
Peptídeos/química , Motivos de Aminoácidos , Cristalografia por Raios X , Modelos Moleculares , Ressonância Magnética Nuclear Biomolecular , Estrutura Secundária de Proteína
6.
Chem Commun (Camb) ; 48(78): 9747-9, 2012 Oct 09.
Artigo em Inglês | MEDLINE | ID: mdl-22914747

RESUMO

Two folded peptides featuring carboxamide and sulfonamide at the core of the peptide fold have been shown to possess almost similar conformational features, despite the well-known fact that carboxamides and sulfonamides have strikingly different hydrogen-bonding and geometrical preferences.


Assuntos
Amidas/química , Peptídeos/química , Sulfonamidas/química , Cristalografia por Raios X , Modelos Moleculares , Estrutura Molecular , Conformação Proteica , Dobramento de Proteína
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