Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Chips are down as Manchester makes protein scanning breakthrough

25.08.2008
Scientists at The University of Manchester have developed a new and fast method for making biological ‘chips’ – technology that could lead to quick testing for serious diseases, fast detection of MRSA infections and rapid discovery of new drugs.

Researchers working at the Manchester Interdisciplinary Biocentre (MIB) and The School of Chemistry have unveiled a new technique for producing functional ‘protein chips’ in a paper in the Journal of the American Chemical Society (JACS), published online today (22 August 2008).

Protein chips – or ‘protein arrays’ as they are more commonly known – are objects such as slides that have proteins attached to them and allow important scientific data about the behaviour of proteins to be gathered.

Functional protein arrays could give scientists the ability to run tests on tens of thousands of different proteins simultaneously, observing how they interact with cells, other proteins, DNA and drugs.

As proteins can be placed and located precisely on a ‘chip’, it would be possible to scan large numbers of them at the same time but then isolate the data relating to individual proteins.

These chips would allow large amounts of data to be generated with the minimum use of materials – especially rare proteins that are only available in very small amounts.

The Manchester team of Dr Lu Shin Wong, Dr Jenny Thirlway and Prof Jason Micklefield say the technical challenges of attaching proteins in a reliable way have previously held back the widespread application and development of protein chips.

Existing techniques for attaching proteins often results in them becoming fixed in random orientations, which can cause them to become damaged and inactive.

Current methods also require proteins to be purified first – and this means that creating large and powerful protein arrays would be hugely costly in terms of time, manpower and money.

Now researchers at The University of Manchester say they have found a reliable new way of attaching active proteins to a chip.

Biological chemists have engineered modified proteins with a special tag, which makes the protein attach to a surface in a highly specified way and ensures it remains functional.

The attachment occurs in a single step in just a few hours – unlike with existing techniques – and requires no prior chemical modification of the protein of interest or additional chemical steps.

Prof Jason Micklefield from the School of Chemistry, said: “DNA chips have revolutionised biological and medical science. For many years scientists have tried to develop similar protein chips but technical difficulties associated with attaching large numbers of proteins to surfaces have prevented their widespread application.

“The method we have developed could have profound applications in the diagnosis of disease, screening of new drugs and in the detection of bacteria, pollutants, toxins and other molecules.”

Researchers from The University of Manchester are currently working as part of a consortium of several universities on a £3.1 million project which is aiming to develop so-called ‘nanoarrays’.

These would be much smaller than existing ‘micro arrays’ and would allow thousands more protein samples to be placed on a single ‘chip’, reducing cost and vastly increasing the volume of data that could be simultaneously collected.

This project, which involves the universities of Manchester, Sheffield, Nottingham and Glasgow, is being supported by Research Councils UK (RCUK), the umbrella body for academic research funding in the UK.

Jon Keighren | alfa
Further information:
http://www.manchester.ac.uk

More articles from Life Sciences:

nachricht Nanoparticle Exposure Can Awaken Dormant Viruses in the Lungs
16.01.2017 | Helmholtz Zentrum München - Deutsches Forschungszentrum für Gesundheit und Umwelt

nachricht Cholera bacteria infect more effectively with a simple twist of shape
13.01.2017 | Princeton University

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Interfacial Superconductivity: Magnetic and superconducting order revealed simultaneously

Researchers from the University of Hamburg in Germany, in collaboration with colleagues from the University of Aarhus in Denmark, have synthesized a new superconducting material by growing a few layers of an antiferromagnetic transition-metal chalcogenide on a bismuth-based topological insulator, both being non-superconducting materials.

While superconductivity and magnetism are generally believed to be mutually exclusive, surprisingly, in this new material, superconducting correlations...

Im Focus: Studying fundamental particles in materials

Laser-driving of semimetals allows creating novel quasiparticle states within condensed matter systems and switching between different states on ultrafast time scales

Studying properties of fundamental particles in condensed matter systems is a promising approach to quantum field theory. Quasiparticles offer the opportunity...

Im Focus: Designing Architecture with Solar Building Envelopes

Among the general public, solar thermal energy is currently associated with dark blue, rectangular collectors on building roofs. Technologies are needed for aesthetically high quality architecture which offer the architect more room for manoeuvre when it comes to low- and plus-energy buildings. With the “ArKol” project, researchers at Fraunhofer ISE together with partners are currently developing two façade collectors for solar thermal energy generation, which permit a high degree of design flexibility: a strip collector for opaque façade sections and a solar thermal blind for transparent sections. The current state of the two developments will be presented at the BAU 2017 trade fair.

As part of the “ArKol – development of architecturally highly integrated façade collectors with heat pipes” project, Fraunhofer ISE together with its partners...

Im Focus: How to inflate a hardened concrete shell with a weight of 80 t

At TU Wien, an alternative for resource intensive formwork for the construction of concrete domes was developed. It is now used in a test dome for the Austrian Federal Railways Infrastructure (ÖBB Infrastruktur).

Concrete shells are efficient structures, but not very resource efficient. The formwork for the construction of concrete domes alone requires a high amount of...

Im Focus: Bacterial Pac Man molecule snaps at sugar

Many pathogens use certain sugar compounds from their host to help conceal themselves against the immune system. Scientists at the University of Bonn have now, in cooperation with researchers at the University of York in the United Kingdom, analyzed the dynamics of a bacterial molecule that is involved in this process. They demonstrate that the protein grabs onto the sugar molecule with a Pac Man-like chewing motion and holds it until it can be used. Their results could help design therapeutics that could make the protein poorer at grabbing and holding and hence compromise the pathogen in the host. The study has now been published in “Biophysical Journal”.

The cells of the mouth, nose and intestinal mucosa produce large quantities of a chemical called sialic acid. Many bacteria possess a special transport system...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

12V, 48V, high-voltage – trends in E/E automotive architecture

10.01.2017 | Event News

2nd Conference on Non-Textual Information on 10 and 11 May 2017 in Hannover

09.01.2017 | Event News

Nothing will happen without batteries making it happen!

05.01.2017 | Event News

 
Latest News

Water - as the underlying driver of the Earth’s carbon cycle

17.01.2017 | Earth Sciences

Interfacial Superconductivity: Magnetic and superconducting order revealed simultaneously

17.01.2017 | Materials Sciences

Smart homes will “LISTEN” to your voice

17.01.2017 | Architecture and Construction

VideoLinks
B2B-VideoLinks
More VideoLinks >>>