Chemoselective immobilization of peptides on abiotic and cell surfaces at controlled densities
We report herein a new and enabling approach for decorating both abiotic and cell surfaces with the extracellular matrix IKVAV peptide in a site-specific manner using strain promoted azide-alkyne cycloaddition. A cyclooctyne-derivatized IKVAV peptide was synthesized and immobilized on the surface of...
Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 26(2010), 11 vom: 01. Juni, Seite 7675-8 |
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1. Verfasser: | |
Weitere Verfasser: | , , , , , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2010
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Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
Schlagworte: | Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Peptides |
Zusammenfassung: | We report herein a new and enabling approach for decorating both abiotic and cell surfaces with the extracellular matrix IKVAV peptide in a site-specific manner using strain promoted azide-alkyne cycloaddition. A cyclooctyne-derivatized IKVAV peptide was synthesized and immobilized on the surface of pancreatic islets through strain-promoted azide-alkyne cycloaddition with cell surface azides generated by the electrostatic adsorption of a cytocompatible poly(L-lysine)-graft-poly(ethylene glycol) (PLL-g-PEG) copolymer bearing azido groups (PP-N(3)). Both "one-pot" and sequential addition of PP-N(3) and a cyclooctyne-derivatized IKVAV peptide conjugate enabled efficient modification of the pancreatic islet surface in less than 60 min. The ability to bind peptides at controlled surface densities was demonstrated in a quantitative manner using microarrays. Additionally, the technique is remarkably rapid and highly efficient, opening new avenues for the molecular engineering of cellular interfaces and protein and peptide microarrays |
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Beschreibung: | Date Completed 08.09.2010 Date Revised 20.10.2021 published: Print Citation Status MEDLINE |
ISSN: | 1520-5827 |
DOI: | 10.1021/la101192v |