A synthetic zipper peptide motif orchestrated via co-operative interplay of hydrogen bonding, aromatic stacking, and backbone chirality.
J Am Chem Soc
; 135(31): 11477-80, 2013 Aug 07.
Article
en En
| MEDLINE
| ID: mdl-23865816
Here, we report on a new class of synthetic zipper peptide which assumes its three-dimensional zipper-like structure via a co-operative interplay of hydrogen bonding, aromatic stacking, and backbone chirality. Structural studies carried out in both solid- and solution-state confirmed the zipper-like structural architecture assumed by the synthetic peptide which makes use of unusually remote inter-residual hydrogen-bonding and aromatic stacking interactions to attain its shape. The effect of chirality modulation and the extent of noncovalent forces in the structure stabilization have also been comprehensively explored via single-crystal X-ray diffraction and solution-state NMR studies. The results highlight the utility of noncovalent forces in engineering complex synthetic molecules with intriguing structural architectures.
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1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
Idioma:
En
Revista:
J Am Chem Soc
Año:
2013
Tipo del documento:
Article
País de afiliación:
India
Pais de publicación:
Estados Unidos