Non-aromatic fluorescence from single α-helical peptides

González González, Carmen; López Blanco, Roi; González Vera, Juan Antonio; Melle Franco, Manuel; Orte Gutiérrez, Ángel; Vazquez, M. Eugenio

doi:10.1016/j.xcrp.2025.102631

1-s2.0-S2666386425002309-main.pdf (4.662Mb)

Identificadores

URI: https://hdl.handle.net/10481/105588

DOI: 10.1016/j.xcrp.2025.102631

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Editorial

Elsevier

Fecha

2025-06-18

Referencia bibliográfica

González-González, C., Lopez-Blanco, R., González-Vera, J. A., D’Ingiullo, S., Bouzada, D., Melle-Franco, M., Orte, A., & Vázquez, M. E. (2025). Non-aromatic fluorescence from single α-helical peptides. Cell Reports. Physical Science, 6(6), 102631. https://doi.org/10.1016/j.xcrp.2025.102631

Patrocinador

MCIN/AEI/10.13039/501100011033 / ERDF (PID2021-127702NB-I00 and PID2020-114256RBI00); MCIN/AEI/10.13039/501100011033 and the European Union NextGenerationEU/PRTR (TED2021-131641B-C41); FEDER / Junta de Andalucía (P21_00212); Xunta de Galicia (ED431G 2023/03); Xunta de Galicia / ERDF (ED431C 2021/29); FCT/MCTES (PIDDAC); European Union’s Horizon 2020 (grant agreement no. 964593)

Resumen

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 nonaromatic 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

Colecciones

OpenAIRE (Open Access Infrastructure for Research in Europe)

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