Non-aromatic fluorescence from single α-helical peptides
We describe a systematic analysis of non-aromatic fluorescence (NAF)-emitting peptides in solution and show that short peptides derived from zwitterionic single α helices (SAHs), formed exclusively by non-aromatic lysine and glutamic acid residues, are UV active and luminescent at near-UV wavelength...
| Autores: | , , , , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2025 |
| País: | España |
| Institución: | Universidad de Santiago de Compostela (USC) |
| Repositorio: | Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela |
| Idioma: | inglés |
| OAI Identifier: | oai:minerva.usc.gal:10347/44485 |
| Acceso en línea: | https://hdl.handle.net/10347/44485 |
| Access Level: | acceso abierto |
| Palabra clave: | Peptides Luminescence Single α-helixz Witterions Non-aromatic fluorescence Intrinsic fluorescence 230224 Péptidos 221007 Espectroscopia electrónica 221020 Espectroscopia molecular 230105 Espectroscopia de emisión |
| Sumario: | We describe a systematic analysis of non-aromatic fluorescence (NAF)-emitting peptides in solution and show that short peptides derived from zwitterionic single α helices (SAHs), formed exclusively by non-aromatic lysine and glutamic acid residues, are UV active and luminescent at near-UV wavelengths in solution (λexc = 320 nm; λem ≈ 420 nm). We also show that their emission depends on the α-helical folding, which favors intramolecular through-space interactions between the Lys/Glu side chains, and that conservative mutations, such as the replacement of Lys by Orn or Arg, strongly influence the NAF emission |
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