Department of Biophysics

Research

The Biophysics Department conducts interdisciplinary research at the interface of biomolecular function, physical chemistry and radiochemistry. The activities contribute to the Helmholtz Research Programmes Nuclear Safety and Cancer Research in the Helmholtz-Association. We are member of the Cluster of Excellence "Physics of Life" (PoL) in Dresden. 

We are particularly interested in:

  • structural and dynamic aspects of biomembranes
  • conformational transitions in membrane proteins
  • interactions between (radio)metals and biomolecules
  • effects of metals and radionuclides on the metabolism of microorganisms (Televised MDR report)

Education

The Biophysics department participates in the Dresden International Graduate School for Biomedicine and Bioengineering (DIGS-BB) supported by the Excellence Initiative of the German federal and state governments.

Practicals on Molecular Spectroscopy and Calorimetry are offered. The following lectures are held at the technische Universität Dresden and are elgible for the Master Specialization "Soft Condensed Matter and Biological Physics":

  • Biological Thermodynamics (English, summer semester)
  • Biophysical Methods (German, winter semester)

Seminar lectures  for the International BIOTEC-Master Programme,

  • Vibrational Spectroscopy (English)
  • Absorption and Fluorescence Spectroscopy (English)

Experimental Methods

  • Fourier transform infrared spectroscopy
  • Circular dichroism
  • Static and time-resolved fluorescence spectroscopy
  • Calorimetry
  • Mass-Spectroscopy

Spectroscopic data are evaluated in combination with Density Functional Theory to understand photochemoical and photophysical properties of organic complexes of actinides.

Latest publication

Synthesis of two methylolanthanin derivatives and the investigation of their lanthanide and iron binding capabilities

Mertens, M. W.; Hügel, S. L.; Hagen, O.; Gutenthaler-Tietze, S. M.; Weis, P.; Drobot, B.; Daumann, L. J.

Abstract

Lanthanides (Lns) have recently been recognized as essential cofactors for certain bacterial enzymes, such as the methanol dehydrogenase (MDH), yet their poor bioavailability under physiological conditions has long suggested the existence of Ln-binding metallophores termed lanthanophores. In this context methylolanthanin (MLL), a chelator which is potentially involved in Ln-uptake of methylotrophic bacteria, was recently isolated and characterized. Herein we synthesized, two novel MLL derivatives, ortho- and meta-MLL, for comparative studies in order to gain a deeper insight into the unusual 4-hydroxy benzoate moiety of native para-MLL. For this we implemented UV-vis titrations, time-resolved laser-induced fluorescence spectroscopy (TRLFS) and ion mobility spectrometry-mass spectrometry (IMS-MS) complemented by density functional theory (DFT) calculations to investigate metal-binding behavior in both solution and gas phase to trivalent Lns. As our binding studies revealed that both artificial chelators tend to precipitate Lns similarly to the native para-MLL under biologically relevant conditions (pH 6.0), rather than solubilizing them, the solubility products of their Eu3+ complexes were determined. Due to structural resemblance of the MLL derivatives to the siderophore rhodopetrobactin B (RPB B), we also investigated iron binding. In this regard ortho-MLL stood out in our analysis and showed a distinctly different binding behavior than the other two derivatives.

Related publications

Permalink: https://www.hzdr.de/publications/Publ-43584

More publications

Team

Head

NameBld./Office+49 351 260Email
Dr. Björn Drobot801/P3022978
b.drobotAthzdr.de

Employees

NameBld./Office+49 351 260Email
Dr. Lisa Nucke801/P3033375
l.nuckeAthzdr.de
Prof. Dr. Satoru Tsushima801/P3022978
s.tsushimaAthzdr.de

Physical Chemistry of Biomolecular Condensates

Head

NameBld./Office+49 351 260Email
Dr. Ellen Adams801/P3012911
e.adamsAthzdr.de

Employees

NameBld./Office+49 351 260Email
Likhitha Chakra Priya Pulibandla801/P3033375
l.pulibandlaAthzdr.de
Manthan Rajm.rajAthzdr.de