Jan Bieschke, Ph.D.

Assistant Professor
Biomedical Engineering

Biochemistry, Biophysics, and Structural Biology Program

  • 314-935-7038

  • 314-935-3959

  • 1097

  • Brauer Hall, Room 2033

  • bieschke@WUSTL.EDU

  • http://blab.bme.wustl.edu/

  • Protein folding, Parkinson`s, Alzheimer`s, microscopy, biophysics

  • I study protein folding and misfolding and how these processes can lead to age-related disease

Research Abstract:

Professor Bieschke’s research focuses on the processes of protein folding and misfolding and how these processes can lead to widespread aging-related diseases such as Alzheimer’s and Parkinson’s disease. Self-assembly of proteins seems to be a generic process but results in insoluble fibrillar structures that can be toxic to the cell but can also have unique material properties. Professor Bieschke aims to dissect and influence these self-assembly processes using biophysical tools such as single molecule fluorescence, atomic force microscopy and sub-diffraction microscopy, in order to develop new strategies to counteract protein misfolding diseases.

Selected Publications:

Bieschke J & Herbst M, et al. (2012) Small molecule conversion of toxic oligomers to non-toxic beta-sheet-rich amyloid fibrils. Nature Chem Biol 8:93-101.

Sommer AP, Bieschke J, Friedrich RP, Zhu D, Wanker EE, Mereles D, Fecht HJ, Hunstein W. (2012) Irradiation With 670 nm Light In Combination With EGCG Therapy Reduces Alzheimer Disease Amyloid-beta Aggregation in Human Neuroblastoma Cells. Photomedicine and Laser Surgery 30:54-60.

Lopez Del Amo JM, Fink U, Dasari M, Grelle G, Wanker EE, Bieschke J, Reif B. (2012) Structural Properties of EGCGInduced, Nontoxic Alzheimer`s Disease Aβ Oligomers. J Mol Biol. 2012 [Epub ahead of print]

Bieschke J, Russ J, Ehrnhoefer D, Wanker EE. (2010) EGCG remodels preformed -sheet rich amyloid fibrils and reduces toxicity. PNAS 107:7710-5.

Ehrnhoefer DA & Bieschke J, Bddrich A, Herbst M, Engemann S, Lurz R, Pastoris A, Wanker EE. (2008) EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nature Struct Mol Biol. 2008 15:558-66.

Cohen E & Bieschke J, Perciavalle R, Kelly JW, Dillin A. (2006) Insulin-like signaling couples the aging process and toxic protein aggregation by regulating opposite detoxification activities. Science 313:1604-10.

Bieschke J & Giese A, Schulz-Schaeffer W, Zerr I, Poser S, Eigen M, Kretzschmar H. (2000) Ultrasensitive detection of pathological prion protein aggregates by dual-color scanning for intensely fluorescent targets. Proc Natl Acad Sci U S A 97(10):5468-73.

Last Updated: 8/9/2012 5:26:57 PM

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