Januar 11, 2018

Posterpräsentation auf dem „Düsseldorf-Jülich-Symposium on Neurodegenerative Diseases“

Auf dem diesjährigen „Düsseldorf-Jülich-Symposium on Neurodegenerative Diseases“, einer der wichtigsten wissenschaftlichen Konferenzen zum Thema Alzheimer, hat Marwa Malhis als Doktorandin der AG Funke ihre Daten im Zuge einer Posterpräsentation interessierten Wissenschaftlern vorgestellt.

Im Rahmen der experimentellen Doktorarbeit werden mittels Phagendisplay spezifische Peptide ermittelt, die eine Fibrillenbildung des Tau-Proteins verhindern. Eben diese wird als Ursache für die Entstehung der Alzheimer-Erkrankung vermutet.


Selection of tau protein binding peptides with potential for therapy of Alzheimer’s

Marwa Malhis, Susanne Aileen Funke

Institut für Bioanalytik, Hochschule für Angewandte Wissenschaften, Coburg, Germany

Alzheimer’s disease (AD) is a slowly progressing, irreversible neurodegenerative disease. It is the most common cause of dementia in the elderly, accounting for about 60% of all dementias. AD is characterized clinically by loss of memory function and other cognitive deficits, including impaired judgment and decision making. The disease is pathologically characterized by the accumulation of abnormal aggregates, i. e. amyloid plaques composed of the β-amyloid peptide (Aβ), and neurofibrillary tangles composed of the microtubule-associated protein tau. Both, Aβ plaques and intracellular neurofibrillary tangles, are considered the pathological hallmarks of AD.

These hallmarks offer potential „targets“ for new drugs to stop or slow the progress of the disease. Here, we focus on the inhibition of tau aggregation. Using phage display, we develop specific peptides that bind to the tau protein for inhibition of tau fibril formation. The tau-binding peptides were identified by affinity selection (called biopanning). For biopanning, a phage library was incubated on a tau-coated surface, followed by extensive washing to remove non-specific phages. Four rounds of biopanning were performed in order to obtain phages that bind with high affinity to tau. Enrichment ELISA and single phage ELISA experiments indicate the success of the phage display selection. Currently, we investigate the potential of the displayed peptides to inhibit the aggregation of tau.