dc.contributor.author |
Misra, Rajkumar |
en_US |
dc.contributor.author |
Reja, Rahi M. |
en_US |
dc.contributor.author |
Narendra, Lagumaddepalli V. |
en_US |
dc.contributor.author |
George, Gijo |
en_US |
dc.contributor.author |
Raghothama, Srinivasarao |
en_US |
dc.contributor.author |
GOPI, HOSAHUDYA N. |
en_US |
dc.date.accessioned |
2019-04-26T09:12:30Z |
|
dc.date.available |
2019-04-26T09:12:30Z |
|
dc.date.issued |
2016-06 |
en_US |
dc.identifier.citation |
Chemical Communications, 52(61), 9597-9600. |
en_US |
dc.identifier.issn |
1359-7345 |
en_US |
dc.identifier.issn |
1364-548X |
en_US |
dc.identifier.uri |
http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/2501 |
|
dc.identifier.uri |
https://doi.org/10.1039/C6CC04502B |
en_US |
dc.description.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. |
en_US |
dc.language.iso |
en |
en_US |
dc.publisher |
Royal Society of Chemistry |
en_US |
dc.subject |
Exploring structural features |
en_US |
dc.subject |
Folded peptide |
en_US |
dc.subject |
Architectures |
en_US |
dc.subject |
Construction of nanomaterials |
en_US |
dc.subject |
Artificial building |
en_US |
dc.subject |
2016 |
en_US |
dc.title |
Exploring structural features of folded peptide architectures in the construction of nanomaterials |
en_US |
dc.type |
Article |
en_US |
dc.contributor.department |
Dept. of Chemistry |
en_US |
dc.identifier.sourcetitle |
Chemical Communications |
en_US |
dc.publication.originofpublisher |
Foreign |
en_US |