Peptide-mediated constructs of quantum dot nanocomposites for enzymatic control of nonradiative energy transfer
buir.contributor.author | Demir, Hilmi Volkan | |
buir.contributor.orcid | Demir, Hilmi Volkan|0000-0003-1793-112X | |
dc.citation.epage | 1539 | en_US |
dc.citation.issueNumber | 4 | en_US |
dc.citation.spage | 1530 | en_US |
dc.citation.volumeNumber | 11 | en_US |
dc.contributor.author | Seker U.O.S. | en_US |
dc.contributor.author | Ozel, T. | en_US |
dc.contributor.author | Demir, Hilmi Volkan | en_US |
dc.date.accessioned | 2016-02-08T09:53:34Z | |
dc.date.available | 2016-02-08T09:53:34Z | |
dc.date.issued | 2011 | en_US |
dc.department | Department of Electrical and Electronics Engineering | en_US |
dc.department | Institute of Materials Science and Nanotechnology (UNAM) | en_US |
dc.description | Supporting Information: The details of preparation of peptide, buffer solutions, and nanocrystals, layer-by-layer assembly, isothermal titration calorimetry, circular dichroism spectroscopy, quartz crystal microbalance, atomic force microscopy, and time-resolved photoluminescence studies, and protease digestion and control experiments. | en_US |
dc.description.abstract | A bottom-up approach for constructing colloidal semiconductor quantum dot (QDot) nanocomposites that facilitate nonradiative Förster-type resonance energy transfer (FRET) using polyelectrolyte peptides was proposed and realized. The electrostatic interaction of these polypeptides with altering chain lengths was probed for thermodynamic, structural, and morphological aspects. The resulting nanocomposite film was successfully cut with the protease by digesting the biomimetic peptide layer upon which the QDot assembly was constructed. The ability to control photoluminescence decay lifetime was demonstrated by proteolytic enzyme activity, opening up new possibilities for biosensor applications. | en_US |
dc.description.provenance | Made available in DSpace on 2016-02-08T09:53:34Z (GMT). No. of bitstreams: 1 bilkent-research-paper.pdf: 70227 bytes, checksum: 26e812c6f5156f83f0e77b261a471b5a (MD5) Previous issue date: 2011 | en |
dc.identifier.doi | 10.1021/nl104295b | en_US |
dc.identifier.issn | 1530-6984 | |
dc.identifier.uri | http://hdl.handle.net/11693/21958 | |
dc.language.iso | English | en_US |
dc.publisher | American Chemical Society | en_US |
dc.relation.isversionof | http://dx.doi.org/10.1021/nl104295b | en_US |
dc.source.title | Nano Letters | en_US |
dc.subject | Nanobiotechnology | en_US |
dc.subject | Nanocomposites | en_US |
dc.subject | Nonradiative energy transfer | en_US |
dc.subject | polypeptides | en_US |
dc.subject | Proteolytic | en_US |
dc.subject | Quantum dots | en_US |
dc.subject | Biomimetic peptides | en_US |
dc.subject | Biosensor applications | en_US |
dc.subject | Bottom up approach | en_US |
dc.subject | Electrostatic interactions | en_US |
dc.subject | Enzymatic control | en_US |
dc.subject | Morphological aspects | en_US |
dc.subject | Non-radiative | en_US |
dc.subject | Biosensors | en_US |
dc.title | Peptide-mediated constructs of quantum dot nanocomposites for enzymatic control of nonradiative energy transfer | en_US |
dc.type | Article | en_US |
Files
Original bundle
1 - 2 of 2
Loading...
- Name:
- Peptide-Mediated Constructs of Quantum Dot Nanocomposites for Enzymatic Control of Nonradiative Energy Transfer.pdf
- Size:
- 4.83 MB
- Format:
- Adobe Portable Document Format
- Description:
- Full printable version
Loading...
- Name:
- nl104295b_si_001
- Size:
- 213.5 KB
- Format:
- Adobe Portable Document Format
- Description: