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DC Field | Value | Language |
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dc.contributor.author | Misra, Rajkumar | en_US |
dc.contributor.author | Sharma, Aman | en_US |
dc.contributor.author | Shirast, Anjali | en_US |
dc.contributor.author | GOPI, HOSAHUDYA N. | en_US |
dc.date.accessioned | 2019-07-01T05:33:51Z | |
dc.date.available | 2019-07-01T05:33:51Z | |
dc.date.issued | 2017-08 | en_US |
dc.identifier.citation | Langmuir, 33 (31),7762-7768. | en_US |
dc.identifier.issn | 0743-7463 | en_US |
dc.identifier.issn | 1520-5827 | en_US |
dc.identifier.uri | http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/3237 | - |
dc.identifier.uri | https://doi.org/10.1021/acs.langmuir.7b01283 | en_US |
dc.description.abstract | We are reporting a spontaneous supramolecular assembly of backbone engineered γ-peptide scaffold and its utility in the immobilization of semiconductor quantum dots and in cell culture. The stimulating feature of this γ-peptide scaffold is that it efficiently gelates both aqueous phosphate buffers and aromatic organic solvents. A comparative and systematic investigation reveals that the greater spontaneous self-aggregation property of γ-peptide over the α- and β-peptide analogues is mainly due to the backbone flexibility, increased hydrophobicity, and π–π stacking of γ-phenylalanine residues. The hydrogels and organogels obtained from the γ-peptide scaffold have been characterized through field emission scanning electron microscopy (FE-SEM), transmission electron microscopy (TEM), FT-IR, circular dichroism (CD), wide-angle X-ray diffraction, and rheometric study. Additionally, the peptide hydrogel has displayed a stimuli-responsive and thixotropic signature, which leads to the injectable hydrogels. 2D cell culture studies using normal and cancer cell lines reveal the biocompatibility of γ-peptide hydrogels. Further, the immobilization of semiconductor core–shell quantum dots in the transparent γ-peptide organogels showed ordered arrangement of quantum dots along the peptide fibrillar network with retaining photophysical property. Overall, γ-peptide scaffolds may serve as potential templates for the design of new functional biomaterials. | en_US |
dc.language.iso | en | en_US |
dc.publisher | American Chemical Society | en_US |
dc.subject | Backbone Engineered | en_US |
dc.subject | γ- Peptide Amphitropic Gels | en_US |
dc.subject | Immobilization | en_US |
dc.subject | Semiconductor Quantum Dots | en_US |
dc.subject | 2D Cell Culture | en_US |
dc.subject | Quantum dots | en_US |
dc.subject | 2017 | en_US |
dc.title | Backbone Engineered γ-Peptide Amphitropic Gels for Immobilization of Semiconductor Quantum Dots and 2D Cell Culture | en_US |
dc.type | Article | en_US |
dc.contributor.department | Dept. of Chemistry | en_US |
dc.identifier.sourcetitle | Langmuir | en_US |
dc.publication.originofpublisher | Foreign | en_US |
Appears in Collections: | JOURNAL ARTICLES |
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