Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Scientists overcome nanotech hurdle

13.08.2008
When you make a new material on a nanoscale how can you see what you have made?

A team lead by a Biotechnology and Biological Sciences research Council (BBSRC) fellow has made a significant step toward overcoming this major challenge faced by nanotechnology scientists.

With new research published today (13 August) in ChemBioChem, the team from the University of Liverpool, The School of Pharmacy (University of London) and the University of Leeds, show that they have developed a technique to examine tiny protein molecules called peptides on the surface of a gold nanoparticle.

This is the first time scientists have been able to build a detailed picture of self-assembled peptides on a nanoparticle and it offers the promise of new ways to design and manufacture novel materials on the tiniest scale - one of the key aims of nanoscience.

Engineering new materials through assembly of complex, but tiny, components is difficult for scientists. However, nature has become adept at engineering nanoscale building blocks, e.g. proteins and RNA. These are able to form dynamic and efficient nanomachines such as the cell's protein assembly machine (the ribosome) and minute motors used for swimming by bacteria. The BBSRC-funded team, led by Dr Raphaël Lévy, has borrowed from nature, developing a way of constructing complex nanoscale building blocks through initiating self-assembly of peptides on the surface of a metal nanoparticle. Whilst this approach can provide a massive number and diversity of new materials relatively easily, the challenge is to be able to examine the structure of the material.

Using a chemistry-based approach and computer modelling, Dr Lévy has been able to measure the distance between the peptides where they sit assembled on the gold nanoparticle. The technique exploits the ability to distinguish between two types of connection or 'cross-link' - one that joins different parts of the same molecule (intramolecular), and another that joins together two separate molecules (intermolecular). As two peptides get closer together there is a transition between the two different types of connection. Computer simulations allow the scientists to measure the distance at which this transition occurs, and therefore to apply it as a sort of molecular ruler. Information obtained through this combination of chemistry and computer molecular dynamics shows that the interactions between peptides leads to a nanoparticle that is relatively organized, but not uniform. This is the first time it has been possible to measure distances between peptides on a nanoparticle and the first time computer simulations have been used to model a single layer of self-assembled peptides.

Dr Lévy said: "As nanotechnology scientists we face a challenge similar to the one faced by structural biologists half a century ago: determining the structure with atomic scale precision of a whole range of nanoscale materials. By using a combination of chemistry and computer simulation we have been able to demonstrate a method by which we can start to see what is going on at the nanoscale.

"If we can understand how peptides self-assemble at the surface of a nanoparticle, we can open up a route towards the design and synthesis of nanoparticles that have complex surfaces. These particles could find applications in the biomedical sciences, for example to deliver drugs to a particular target in the body, or to design sensitive diagnostic tests. In the longer term, these particles could also find applications in new generations of electronic components."

Professor Nigel Brown, BBSRC Director of Science and Technology, said: "Bionanotechnology holds great promise for the future. We may be able to create stronger, lighter and more durable materials, or new medical applications. Basic science and techniques for working at the nanoscale are providing the understanding that will permit future such applications of bionanotechnology."

Press Office | alfa
Further information:
http://www3.interscience.wiley.com/journal/121376845/abstract
http://www.bbsrc.ac.uk/media/releases/2008/080813_nanotech.html

More articles from Life Sciences:

nachricht Seeing on the Quick: New Insights into Active Vision in the Brain
15.08.2018 | Eberhard Karls Universität Tübingen

nachricht New Approach to Treating Chronic Itch
15.08.2018 | Universität Zürich

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Unraveling the nature of 'whistlers' from space in the lab

A new study sheds light on how ultralow frequency radio waves and plasmas interact

Scientists at the University of California, Los Angeles present new research on a curious cosmic phenomenon known as "whistlers" -- very low frequency packets...

Im Focus: New interactive machine learning tool makes car designs more aerodynamic

Scientists develop first tool to use machine learning methods to compute flow around interactively designable 3D objects. Tool will be presented at this year’s prestigious SIGGRAPH conference.

When engineers or designers want to test the aerodynamic properties of the newly designed shape of a car, airplane, or other object, they would normally model...

Im Focus: Robots as 'pump attendants': TU Graz develops robot-controlled rapid charging system for e-vehicles

Researchers from TU Graz and their industry partners have unveiled a world first: the prototype of a robot-controlled, high-speed combined charging system (CCS) for electric vehicles that enables series charging of cars in various parking positions.

Global demand for electric vehicles is forecast to rise sharply: by 2025, the number of new vehicle registrations is expected to reach 25 million per year....

Im Focus: The “TRiC” to folding actin

Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.

Actin is the most abundant protein in highly developed cells and has diverse functions in processes like cell stabilization, cell division and muscle...

Im Focus: Lining up surprising behaviors of superconductor with one of the world's strongest magnets

Scientists have discovered that the electrical resistance of a copper-oxide compound depends on the magnetic field in a very unusual way -- a finding that could help direct the search for materials that can perfectly conduct electricity at room temperatur

What happens when really powerful magnets--capable of producing magnetic fields nearly two million times stronger than Earth's--are applied to materials that...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

VideoLinks
Industry & Economy
Event News

Within reach of the Universe

08.08.2018 | Event News

A journey through the history of microscopy – new exhibition opens at the MDC

27.07.2018 | Event News

2018 Work Research Conference

25.07.2018 | Event News

 
Latest News

Unraveling the nature of 'whistlers' from space in the lab

15.08.2018 | Physics and Astronomy

Diving robots find Antarctic winter seas exhale surprising amounts of carbon dioxide

15.08.2018 | Earth Sciences

Early opaque universe linked to galaxy scarcity

15.08.2018 | Physics and Astronomy

VideoLinks
Science & Research
Overview of more VideoLinks >>>