Amyloid peptide aggregation near gold interfaces and membranes
The aggregation of peptides into amyloid fibrils, desired or undesired, plays an important role in biological systems. Amyloid-forming peptides are soluble in its native state and aggregate under certain circumstances via intermediates to insoluble fibrils with characteristic cross-β-sheet structure. This aggregation is believed to be connected with several neurodegenerative disorders such as Alzheimer’s disease (AD). However, it is not yet clear if the oligomeric intermediates or the mature fibrils are the toxic species or if amyloid fibrils are just a side product in the development of these diseases.
Continue reading “Talk by T. John at UL (June 13, 2017)”
Effects of the αC-relaxation for PEO and POM: Impact on Crystallization Process, Morphology and Reorganization Behavior
Depending on the presence or absence of an αC-relaxation it is possible to distinguish between crystal-mobile and crystal-fixed semi-crystalline polymers. Only crystal-mobile polymers own a certain chain mobility in the crystalline phase. In contrast to the crystal-fixed polymer Polycaprolactone (PCL), we analyze the impact of the αC-relaxation for two representatives of αC-mobile polymers, Polyethylenoxide (PEO) and Polyoxymethylene (POM), using different methods like SAXS and Flash-/DSC.
Continue reading “Talk by M. Schulz at MLU (May 16, 2017)”
Competition between Electrostatic and Hydrophobic Forces in the Central Core Region of Amyloid β Fibrils
Amyloidogenic peptides aggregated to large molecular assemblies are a hallmark of several diseases including Parkinson’s, Huntington’s, and Alzheimer’s disease as well as type II diabetes. Although each of these diseases gives rise to a very distinctive clinical picture, amyloid fibrils share the cross-β structure as a common structural motif. Within this motif, the peptide strands are linked via lateral β-sheet-turn-β-sheet structures that result in fiber-like aggregates with diameters of a few nanometers and lengths up to several micrometers.
The central question that will be addressed is how electrostatic and hydrophobic interactions compete within the central core region of Aβ(1-40) fibrils. Continue reading “Talk by F. Hoffmann at MLU (April 4, 2017)”
Effect of Different Crowding Agents on Structure and Dynamics of Unfolded Proteins
The interior of a cell is completely filled with molecules like proteins, lipids, RNA, and more which can act as crowders. The so-called macromolecular crowding plays an important role in the dynamics and the structure of proteins, especially unfolded proteins and polypeptide chains.
To investigate the influence of crowder agents on the dynamics and structure of unfolded polypeptide chains we performed time-resolved ensemble FRET experiments with different sizes of crowders and different unfolded polypeptide chains. Continue reading “Talk by P. Enke at MLU (March 14, 2017)”
Serine substitution in Amyloid-β – a possible link between β-Methylamino-L-alanine and Alzheimer’s disease?
In 1944 Guam was recaptured and fortified by US forces. Decades later soldiers that were stationed at Guam developed ALS-PDC (amyotrophic lateral sclerosis–parkinsonism/dementia complex) 50-100 times the incidence of ALS. Also Guam’s natives, the Chamorro, are plagued by severe neurodegenerative diseases. When looking for a possible cause for this phenomenon, scientists soon focused on the neurotoxin BMAA, found in cycad tree fruits, an important food source in Guam. BMAA is a non- proteinogenic amino acid produced by cyanobacteria that can be enriched via the food chain in plants, seafood and higher animals. This is a critical factor because cyanobacteria are known for their excessive blooms not only in marine ecosystems but also in lakes that are used as fresh water source for millions of people.
Continue reading “Talk by A. Korn at UL (February 21, 2017)”
Polymers on Surfaces – or how to catch them all
The talk will feature recent developments in the lab. It focuses mainly on the preparation of thinnest polymer films / single molecules under UHV condition. It introduces the techniques quadrupole mass spectrometry (QMS), quartz microbalance (QMB) and scanning tunneling microscopy (STM) and how their results should lead to a successful preparation. A short overview of what is coming next will be given at the end of the talk.
Location: MLU Halle-Wittenberg, Von-Danckelmann-Platz 3, SR 1.03, 06120 Halle (Saale)
Date and time: 06.12.16 at 3.30pm
Amyloid Beta Aggregation in the Presence of Temperature-Sensitive Polymers
The formation of amyloid fibrils is considered to be one of the main causes for many neurodegenerative diseases, such as Alzheimer’s, Parkinson’s or Huntington’s disease . Current knowledge suggests that amyloid-aggregation represents a nucleation-dependent aggregation process in vitro, where a sigmoidal growth phase follows an induction period. Here, we studied the fibrillation of amyloid β 1-40 (Aβ40) in the presence of thermoresponsive polymers, expected to alter the Aβ40 fibrillation kinetics due to their lower critical solution behavior [2-6]. Continue reading “Talk by Z. Evgrafova at MLU (January 31, 2017)”