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11-16 April 2026
Conference 13006 > Paper 13006-48
Paper 13006-48

Effect of molecular dynamics and internal water contact on the photophysical properties of red pH sensitive proteins

10 April 2024 • 15:50 - 16:10 CEST | Etoile B, Niveau/Level 1

Abstract

This study analyses the pH-dependent time resolved fluorescence of mCardinal and mNeptune, two red-shifted fluorescent proteins with applications in biomedical imaging. We utilized molecular dynamics (MD) simulations to illuminate the influence of water molecules on the proteins´ photophysical properties. In mCardinal, the average fluorescence lifetime markedly rises from 0.95 ns at pH 7.0 to 1.25 ns at pH 5.5. Conversely, mNeptune exhibits a constant fluorescence lifetime, showing no pH sensitivity. Through Decay-Associated Spectra and MD simulations, we correlated mCardinal’s pH-induced lifetime changes with its molecular properties. Despite both proteins being equally stabilized by hydrogen bonds, mCardinal’s chromophore formed more water contacts than mNeptune’s. Additionally, the chromophore’s interactions with specific amino acids varied between the two proteins, suggesting distinct differences in the excited state proton transfer as a crucial mechanism for pH sensitivity.

Presenter

Martin-Luther-Univ. Halle-Wittenberg (Germany)
Author
Martin-Luther-Univ. Halle-Wittenberg (Germany)
Author
Martin-Luther-Univ. Halle-Wittenberg (Germany)
Author
Martin-Luther-Univ. Halle-Wittenberg (Germany)
Author
Leibniz-Institut für Neue Materialien gGmbH (Germany)
Author
Martin-Luther-Univ. Halle-Wittenberg (Germany)
Author
Farzin Ghane Golmohamadi
Martin-Luther-Univ. Halle-Wittenberg (Germany)
Presenter/Author
Martin-Luther-Univ. Halle-Wittenberg (Germany)