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Exploring structural features of folded peptide architectures in the construction of nanomaterials

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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


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