General Method for Peptide Recognition in Water through Bioinspired Complementarity
A general method for peptide recognition has been elusive despite decades of research. Strong binding and selectivity among closely related peptides are necessary for biological applications but have been difficult to achieve with synthetic receptors. With inspiration from highly specific protein-pr...
| Veröffentlicht in: | Chemistry of materials : a publication of the American Chemical Society. - 1998. - 31(2019), 13 vom: 09. Juli, Seite 4889-4896 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2019
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| Zugriff auf das übergeordnete Werk: | Chemistry of materials : a publication of the American Chemical Society |
| Schlagworte: | Journal Article |
| Zusammenfassung: | A general method for peptide recognition has been elusive despite decades of research. Strong binding and selectivity among closely related peptides are necessary for biological applications but have been difficult to achieve with synthetic receptors. With inspiration from highly specific protein-protein and protein-ligand interactions, protein-sized, water-soluble imprinted nanoparticles were prepared via templated polymerization of peptides within cross-linked micelles. Combination of hydrophobic and polar interactions afforded micromolar to submicromolar binding affinities for selected tripeptides. A "golden pair" of functional monomers was identified to enhance both the affinity and selectivity of binding, and enabled differentiation of subtly different sequences including single-point variation of lysine by arginine and insertion of a single glycine at the N- or C-terminus. Biological peptides (β-amyloid peptides) afforded even stronger binding (tens of nanomolar) due to a larger number of complementary interactions between the host and the guest, opening doors to a wide range of biological applications |
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| Beschreibung: | Date Revised 29.03.2024 published: Print-Electronic Citation Status PubMed-not-MEDLINE |
| ISSN: | 0897-4756 |
| DOI: | 10.1021/acs.chemmater.9b01613 |