Short hydrogen bonds enhance nonaromatic protein-related fluorescence

STEPHENS, AMBERLEY D.; QAISRANI, MUHAMMAD NAWAZ; RUGGIERO, MICHAEL T.; DÍAZ MIRÓN, GONZALO; MORZAN, URIEL N.; GONZÁLEZ LEBRERO, MARIANO C.; JONES, SAUL T. E.; POLI, EMILIANO; BOND, ANDREW D.; WOODHAMS, PHILIPPA J.; KLEIST, ELYSE M.; GRISANTI, LUCA; GEBAUER, RALPH; ZEITLER, J. AXEL; CREDGINGTON, DAN; HASSANALI, ALI; KAMINSKI SCHIERLE, GABRIELE S.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

NATL ACAD SCIENCES

Año: 2021 vol. 118

0027-8424

Intrinsic fluorescence of nonaromatic amino acids is a puzzling phenomenon with an enormous potential in biophotonic applications. The physical origins of this effect, however, remain elusive. Herein, we demonstrate how specific hydrogen bond networks can modulate fluorescence. We highlight the key role played by short hydrogen bonds, present in the protein structure, on the ensuing fluorescence. We provide detailed experimental and molecular evidence to explain these unusual nonaromatic optical properties. Our findings should benefit the design of novel optically active biomaterials for applications in biosensing and imaging.