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Exploring structural features of folded peptide architectures in the construction of nanomaterials.
Misra, Rajkumar; Reja, Rahi M; Narendra, Lagumaddepalli V; George, Gijo; Raghothama, Srinivasarao; Gopi, Hosahudya N.
Afiliação
  • Misra R; Department of Chemistry, Indian Institution of Science Education and Research, Dr. Homi Bhabha Road, Pune-411008, India. hn.gopi@iiserpune.ac.in.
  • Reja RM; Department of Chemistry, Indian Institution of Science Education and Research, Dr. Homi Bhabha Road, Pune-411008, India. hn.gopi@iiserpune.ac.in.
  • Narendra LV; NMR Research Center, Indian Institute of Science, Bangalore-560012, India.
  • George G; NMR Research Center, Indian Institute of Science, Bangalore-560012, India.
  • Raghothama S; NMR Research Center, Indian Institute of Science, Bangalore-560012, India.
  • Gopi HN; Department of Chemistry, Indian Institution of Science Education and Research, Dr. Homi Bhabha Road, Pune-411008, India. hn.gopi@iiserpune.ac.in.
Chem Commun (Camb) ; 52(61): 9597-600, 2016 Jul 21.
Article em En | MEDLINE | ID: mdl-27399170
ABSTRACT
We are reporting the influence of foldamer structures on their self-assembled architectures. In a sharp contrast to the ordered α,γ-hybrid 12-helix obtained from 1 1 alternating Aib and γ-Phe, the α,γ-hybrid peptides constituted with α-Phe and 4,4-dimethyl γ-amino acid (Aic) displayed the extended sheet type of conformations in solution and spontaneously self-assembled into thermally and proteolytically stable capsules. In contrast, the conformationally ordered 12-helix self-assembled into a three-dimensional supramolecular polyhedron.

Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2016 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2016 Tipo de documento: Article