Biomolecular Photonics
Prof. Dr. Christoph BISKUP
Prof. Christoph Biskup.
Image: Jan-Peter Kasper (University of Jena)
Prof. Dr. Christoph Biskup
Image: PrivateProf. Dr. Christoph BISKUP
Email: christoph.biskup@uni-jena.de
Phone: +49 3641-9-397800
Fax: +49 3641-9-397802
Prof. Christoph Biskup heads the Biomolecular Photonics Group at Jena University Hospital. His research focuses on the development and application of quantitative fluorescence microscopy techniques for investigating molecular processes in living cells. A particular emphasis lies on multidimensional fluorescence imaging, fluorescence lifetime imaging microscopy (FLIM) and Förster resonance energy transfer (FRET). These techniques provide access not only to the spatial distribution of fluorescent molecules, but also to their photophysical properties, molecular environment and interactions at nanometre length scales.
Research Areas
The Biomolecular Photonics Group develops and applies quantitative fluorescence microscopy techniques for the analysis of molecular processes in living cells. Research interests include:
- Multidimensional and spectrally resolved fluorescence lifetime imaging microscopy (FLIM)
- FLIM-FRET for quantitative analysis of molecular interactions in living cells
- Photophysical characterization of fluorescent proteins and molecular probes
- Optical protein-protein and protein-DNA interaction assays
- Fluorescence-based analysis of ion channels and cellular signalling
- Fluorescent indicators and nanosensors for ions and biomolecules
Teaching Fields
Prof. Biskup is head of the examination committee of the interdisciplinary M.Sc. program Medical Photonics. He gives lectures and courses in:
- Anatomy and physiology for Medical Photonics
- Biological and fluorescence microscopy
- Quantitative fluorescence imaging techniques
- Image processing and analysis
Research Methods
The Biomolecular Photonics Group combines advanced fluorescence microscopy and spectroscopy with molecular and cellular methods. Photonic techniques include:
- Confocal laser scanning fluorescence microscopy
- Fluorescence lifetime imaging microscopy (FLIM)
- FLIM-based Förster resonance energy transfer (FLIM-FRET)
- Spectrally and time-resolved fluorescence microscopy
- Time-correlated single-photon counting (TCSPC)
- Streak-camera-based fluorescence lifetime measurements
- Fluorescence spectroscopy and characterization of fluorescent proteins
- Fluorescence anisotropy and molecular-interaction measurements
- Patch-clamp fluorometry
Recent Research Results
Fluorescence decay surface recorded by using multidimensional fluorescence microscopy techniques. For each voxel of a cell, a time-resolved fluorescence spectrum is recorded.
Illustration: Research group of Christoph BiskupQuantitative fluorescence microscopy provides molecular information beyond the intensity and spatial distribution recorded in conventional fluorescence imaging. In particular, fluorescence lifetime imaging microscopy (FLIM) is sensitive to the photophysical environment of fluorescent molecules and can be combined with Förster resonance energy transfer (FRET) to quantify molecular interactions in living cells.
Recent work of the Biomolecular Photonics Group has applied FLIM-FRET to visualize and quantify protein-protein interactions under physiological conditions. FLIM-FRET measurements were used to analyse interactions between S100A11 and different annexin proteins in living cells and to determine how these interactions depend on calcium binding [1].
The group has further used FLIM-FRET to investigate the regulation of cell-cycle proteins. Measurements of interactions between the cell-cycle regulator p21 and PCNA demonstrated how specific phosphorylation states modify molecular binding in living cells [2]. More recently, FLIM-FRET imaging was used to visualize the influence of p21 and its molecular state on the formation of CDK/cyclin complexes [3].
An important complementary topic is the quantitative characterization of fluorescent proteins themselves. Spectrally and time-resolved fluorescence measurements combined with FLIM-FRET have shown that different translation products of the widely used fluorescent protein mCherry exhibit markedly different photophysical and FRET properties. Such effects need to be considered when fluorescent proteins are used as quantitative molecular reporters [4].
These studies demonstrate how multidimensional fluorescence measurements can translate photophysical observables such as fluorescence lifetime and energy-transfer efficiency into quantitative information on molecular interactions and dynamics in living cells.
[1] Melle et al., FEBS Open Bio 14, 626 (2024).
[2] Melle et al., Biochem. Biophys. Res. Commun. 809, 153508 (2026).
[3] Melle et al., J. Cell Sci., jcs.265097 (2026).
[4] Hoffmann et al., Front. Bioeng. Biotechnol. 13, 1613582 (2025).