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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kumar, Anil | - |
dc.date.accessioned | 2021-10-27T04:11:37Z | - |
dc.date.available | 2021-10-27T04:11:37Z | - |
dc.date.issued | 2007-06-20 | - |
dc.identifier.uri | https://pubs.acs.org/doi/10.1021/jm070416o | - |
dc.identifier.uri | http://dspace.bits-pilani.ac.in:8080/xmlui/handle/123456789/2951 | - |
dc.description.abstract | Tripodal peptide analogues were designed on the basis of the phosphotyrosine binding pocket of the Src SH2 domain and assayed for their ability to bind to fluorescein-labeled phosphopeptides. Fluorescence polarization assays showed that a number of amphipathic linear peptide analogues (LPAs), such as LPA4, bind to fluorescein-labeled GpYEEI (F-GpYEEI). LPA4 was evaluated for potential application in cellular delivery of phosphopeptides. Fluorescence microimaging cellular uptake studies with fluorescein-attached LPA4 (F-LPA4) alone or with the mixture of LPA4 and F-GpYEEI in BT-20 cells showed dramatic increase of the fluorescence intensity in cytosol of cells, indicating that LPA4 can function as a delivery tool of F-GpYEEI across the cell membrane. Fluorescent flow cytometry studies showed the cellular uptake of F-LPA4 in an energy-independent pathway and confirmed the cellular uptake of F-GpYEEI in the presence of LPA4. These studies suggest that amphipathic tripodal peptide analogues, such as LPA4, can be used for cellular delivery of phosphopeptides | en_US |
dc.language.iso | en | en_US |
dc.publisher | ACS | en_US |
dc.subject | Chemistry | en_US |
dc.subject | Cell uptake | en_US |
dc.subject | Peptides and proteins | en_US |
dc.subject | Fluorescence | en_US |
dc.title | Synthesis and evaluation of tripodal peptide analogues for cellular delivery of phosphopeptides | en_US |
Appears in Collections: | Department of Chemistry |
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