Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/1721
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dc.contributor.authorJADHAV, SANDIP V.en_US
dc.contributor.authorSingh, Sumeet K.en_US
dc.contributor.authorReja, Rahi M.en_US
dc.contributor.authorGOPI, HOSAHUDYA N.en_US
dc.date.accessioned2019-02-14T05:05:03Z
dc.date.available2019-02-14T05:05:03Z
dc.date.issued2013-10en_US
dc.identifier.citationChemical Communications, 49(94), 11065-11067.en_US
dc.identifier.issn1359-7345en_US
dc.identifier.issn1364-548Xen_US
dc.identifier.urihttp://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/1721-
dc.identifier.urihttps://doi.org/10.1039/C3CC46652Cen_US
dc.description.abstracthe stability and compatibility of designed coiled coil peptides towards the selective incorporation of γ4-amino acids at the hydrophobic positions of the heptad repeat are studied. Investigations reveal that the low thermal denaturation temperature of γ4-residue mutated coiled coils can be utilized as a mild hyperthermia trigger in liposomes.en_US
dc.language.isoenen_US
dc.publisherRoyal Society of Chemistryen_US
dc.subjectγ-Aminoen_US
dc.subjectα-coiled coilsen_US
dc.subjectThermal triggersen_US
dc.subjectBiocompatibilityen_US
dc.subjectConformationallyen_US
dc.subject2013en_US
dc.titleγ-Amino acid mutated α-coiled coils as mild thermal triggers for liposome deliveryen_US
dc.typeArticleen_US
dc.contributor.departmentDept. of Chemistryen_US
dc.identifier.sourcetitleChemical Communicationsen_US
dc.publication.originofpublisherForeignen_US
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