Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Bacteria disarmer activates fiber formation in Parkinson’s protein

16.02.2012
The same substance that hampers the infection capability of bacteria can hasten the fiber formation of the protein that is involved in the development of Parkinson’s disease.

The study shows how important basic research is to our understanding of possible side effects from drug candidates interacting with various target proteins.

The study was done by researchers at Umeå University in Sweden and is published in the latest issue of the prestigious Journal of the American Chemical Society. The findings surprise all the researchers involved.

Fredrik Almqvist, professor of organic chemistry, working with colleagues at Washington University in St. Louis and the University of Michigan in Ann Arbor, has developed a molecule, FN075, that slows down the infection capability of bacteria. This molecule blocks the growth and function of the hair-like shoots that bacteria use to cause infections. Even though the molecule is not used in any drugs today, this disarming principle could be of great importance in future struggles against resistance to antibiotics.

Interestingly, bacteria’s hair-like shoots are structured according to the same principle as amyloid proteins, improperly folded proteins that accumulate in nerve disorders like Parkinson’s and Alzheimer’s diseases.

“So we tested whether FN 075 could also hamper the formation of amyloids in a protein that is implicated in Parkinson’s disease. But instead it turned out that the molecule boosted the formation of amyloid structures,” says Pernilla Wittung-Stafshede, professor of biological chemistry.

In other words, the same tiny molecule can have exactly the opposite effect depending on what protein it encounters and in what surroundings. The study thus shows that it is important to test for possible side effects that new substances might have on amyloid proteins.

“There seems to be a fine balance between what activities these types of substances hamper and what activities they prompt,” says Pernilla Wittung-Stafshede.

She says it is too early to say whether the effects on the amyloid proteins are positive or negative from a medical perspective. On the other hand, it is clear that molecules like FN075 are key research tools to achieve an understanding of these types of complex processes.

The new findings have inspired the researchers regarding how to continue to design and use small molecules that can affect amyloid formation.

“Perhaps some of the body’s own small metabolites help to trigger amyloid formation in nerve disorders like Parkinson’s and Alzheimer’s,” wonders Fredrik Almqvist, who declares that they will now be following up these findings.

The research is being conducted at the Chemical Biology Centre, KBC, and the Umeå Centre for Microbial Research, UCMR at Umeå University and is based on the combined expertise of the chemists Pernilla Wittung-Stafshede, Magnus Wolf-Watz, and Fredrik Almqvist. Most of the study was carried out by post-doctoral fellows Istvan Horvath, Christoph F. Weise, and Emma Andersson. With the assistance of the KBC platform for nuclear magnetic resonance, NMR, the scientists have been able to study proteins at the atomic level.

For more information, please contact:
Pernilla Wittung-Stafshede, professor of biological chemistry, Department of Chemistry, Chemical Biological Centre, KBC, Umeå University

E-mail: pernilla.wittung@chem.umu.se

Fredrik Almqvist, professor of organic chemistry, Department of Chemistry, Chemical Biological Centre, KBC, and Umeå Centre for Microbial Research, UCMR, Umeå University
Tel: +46 (0)90-7866925
E-mail: fredrik.almqvist@chem.umu.se
Magnus Wolf-Watz, associate professor of chemistry, Department of Chemistry, Chemical Biological Centre, KBC, Umeå University
Tel: +46 (0)90-786 76 90
E-mail: magnus.wolf-watz@chem.umu.se
Original publication:
Istvan Horvath, Christoph Felix Weise, Emma K. Andersson, Erik Chorell, Magnus Sellstedt, Christoffer Bengtsson, Anders Olofsson, Scott J. Hultgren, Matthew R Chapman, Magnus Wolf-Watz, Fredrik Almqvist, and Pernilla EL Wittung-Stafshede. Mechanisms of protein oligomerization: Inhibitor of functional amyloids templates α-synuclein fibrillation. Journal of the American Chemical Society 2012. DOI: 10.1021/ja209829m. 2012-02-09

Karin Wikman | idw
Further information:
http://pubs.acs.org/doi/abs/10.1021/ja209829m
http://www.umu.se

More articles from Life Sciences:

nachricht Historical rainfall levels are significant in carbon emissions from soil
30.05.2017 | University of Texas at Austin

nachricht 3D printer inks from the woods
30.05.2017 | Empa - Eidgenössische Materialprüfungs- und Forschungsanstalt

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: New Method of Characterizing Graphene

Scientists have developed a new method of characterizing graphene’s properties without applying disruptive electrical contacts, allowing them to investigate both the resistance and quantum capacitance of graphene and other two-dimensional materials. Researchers from the Swiss Nanoscience Institute and the University of Basel’s Department of Physics reported their findings in the journal Physical Review Applied.

Graphene consists of a single layer of carbon atoms. It is transparent, harder than diamond and stronger than steel, yet flexible, and a significantly better...

Im Focus: Strathclyde-led research develops world's highest gain high-power laser amplifier

The world's highest gain high power laser amplifier - by many orders of magnitude - has been developed in research led at the University of Strathclyde.

The researchers demonstrated the feasibility of using plasma to amplify short laser pulses of picojoule-level energy up to 100 millijoules, which is a 'gain'...

Im Focus: Can the immune system be boosted against Staphylococcus aureus by delivery of messenger RNA?

Staphylococcus aureus is a feared pathogen (MRSA, multi-resistant S. aureus) due to frequent resistances against many antibiotics, especially in hospital infections. Researchers at the Paul-Ehrlich-Institut have identified immunological processes that prevent a successful immune response directed against the pathogenic agent. The delivery of bacterial proteins with RNA adjuvant or messenger RNA (mRNA) into immune cells allows the re-direction of the immune response towards an active defense against S. aureus. This could be of significant importance for the development of an effective vaccine. PLOS Pathogens has published these research results online on 25 May 2017.

Staphylococcus aureus (S. aureus) is a bacterium that colonizes by far more than half of the skin and the mucosa of adults, usually without causing infections....

Im Focus: A quantum walk of photons

Physicists from the University of Würzburg are capable of generating identical looking single light particles at the push of a button. Two new studies now demonstrate the potential this method holds.

The quantum computer has fuelled the imagination of scientists for decades: It is based on fundamentally different phenomena than a conventional computer....

Im Focus: Turmoil in sluggish electrons’ existence

An international team of physicists has monitored the scattering behaviour of electrons in a non-conducting material in real-time. Their insights could be beneficial for radiotherapy.

We can refer to electrons in non-conducting materials as ‘sluggish’. Typically, they remain fixed in a location, deep inside an atomic composite. It is hence...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

Marine Conservation: IASS Contributes to UN Ocean Conference in New York on 5-9 June

24.05.2017 | Event News

AWK Aachen Machine Tool Colloquium 2017: Internet of Production for Agile Enterprises

23.05.2017 | Event News

Dortmund MST Conference presents Individualized Healthcare Solutions with micro and nanotechnology

22.05.2017 | Event News

 
Latest News

3D printer inks from the woods

30.05.2017 | Life Sciences

How circadian clocks communicate with each other

30.05.2017 | Life Sciences

Graphene and quantum dots put in motion a CMOS-integrated camera that can see the invisible

30.05.2017 | Physics and Astronomy

VideoLinks
B2B-VideoLinks
More VideoLinks >>>