Uracil-amino acid as a scaffold for β-sheet peptidomimetics: Study of photophysics and interaction with BSA protein
| Autor: | Subhendu Sekhar Bag, Afsana Yashmeen |
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| Rok vydání: | 2017 |
| Předmět: |
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Stereochemistry Peptidomimetic Clinical Biochemistry Beta sheet Pharmaceutical Science Peptide 010402 general chemistry 01 natural sciences Biochemistry Pentapeptide repeat Protein Structure Secondary parasitic diseases Drug Discovery Fluorescence Resonance Energy Transfer Animals Amino Acids Uracil Molecular Biology Alanine chemistry.chemical_classification Aza Compounds 010405 organic chemistry Circular Dichroism Organic Chemistry Serum Albumin Bovine 0104 chemical sciences Amino acid Förster resonance energy transfer chemistry Molecular Medicine Cattle Peptidomimetics Two-dimensional nuclear magnetic resonance spectroscopy Protein Binding |
| Zdroj: | Bioorganic & Medicinal Chemistry Letters. 27:5387-5392 |
| ISSN: | 0960-894X |
| DOI: | 10.1016/j.bmcl.2017.11.017 |
| Popis: | We report herein the uracil-di-aza-amino acid ( U r AA ) as a new family of molecular scaffold to induce β-hairpin structure with H-bonded β-sheet conformation in a short peptide. This has been demonstrated in two conceptual fluorescent pentapeptides wherein triazolylpyrenyl alanine and/or triazolylmethoxynapthyl alanine ( TPy Ala Do and/or TMNap Ala Do ) are embedded into two arms of the uracil-amino acid via an intervening leucine. Conformational analysis by CD, IR, variable temperature and 2D NMR spectroscopy reveals the β-hairpin structures for both the peptides. Study of photophysical property reveals that the pentapeptide containing fluorescent triazolyl unnatural amino acids TMNap Ala Do and TPy Ala Do at the two termini exhibits dual path entry to exciplex emission-either via FRET from TMNap Ala Do to TPy Ala Do or via direct excitation of a FRET acceptor, TPy Ala Do . The other pentapeptide with TPy Ala Do / TPy Ala Do pair shows excimer emission. Furthermore, both the peptides maintaining their fundamental photophysics are found to interact with BSA as only a test biomolecule. |
| Databáze: | OpenAIRE |
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