TY - JOUR
T1 - Exploring structural features of folded peptide architectures in the construction of nanomaterials
AU - Misra, Rajkumar
AU - Reja, Rahi M.
AU - Narendra, Lagumaddepalli V.
AU - George, Gijo
AU - Raghothama, Srinivasarao
AU - Gopi, Hosahudya N.
N1 - Publisher Copyright:
© 2016 The Royal Society of Chemistry.
PY - 2016
Y1 - 2016
N2 - 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 11 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.
AB - 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 11 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.
UR - http://www.scopus.com/inward/record.url?scp=84979643793&partnerID=8YFLogxK
U2 - 10.1039/c6cc04502b
DO - 10.1039/c6cc04502b
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AN - SCOPUS:84979643793
SN - 1359-7345
VL - 52
SP - 9597
EP - 9600
JO - Chemical Communications
JF - Chemical Communications
IS - 61
ER -