Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

The assembly of protein strands into fibrils

12.04.2010
The Atomic Force Microscope depicts on its screen the few nanometer thick and few micrometer long fibers as white flexible sticks, crisscrossing the surface on which they are deposited. The very peculiar property of these proteins lies in fact that they can self assemble into complex ribbon-like twisted fibers.

Researchers at ETH Zürich, EPF Lausanne and University of Fribourg have teamed up to take Atomic Force Microscopy images of the fibers and to analyze them using concepts from polymer physics and theoretical modeling.

This combination of expertise has lead them to propose a set of general rules governing the assembly of filaments into thicker and twisted ribbon like fibers. Their results are published in the current issue of the scientific journal "Nature Nanotechnology".

"The model that we propose is extremely precise in its predictions", says Raffaele Mezzenga, Professor of Food and Soft Materials Sciences at the ETH Zürich. "Up to now there was no such exact and general model for the formation of Amyloid fibers", continues Giovanni Dietler, Professor of Physics of Living Matter, at the EPF Lausanne.

The structure of the Amyloid fibers as it was unveiled by the experiments, surprised the researchers. Single proteins build the long filaments and subsequently the filaments assemble side by side to form the ribbon-like twisted fibers.

Mezzenga explains that the ribbon-like structure is the logic consequence of the strong charge carried by the building blocks of the fibers. In fact, the single proteins feel a strong mutual repulsion preventing them to pack and the ribbon structure is the only one that permits to limit this repulsion. Presently one missing information in the present model, is the exact nature of the short range attraction between the building blocks that drives in the first place the assembly among the protein filaments. Scientists agree that along the filaments there are charge-less domains of hydrophobic character (water repellant) that are the source of the short-range attraction. So there is a balance between attractive and repulsive interactions and the results is the ribbon like twisted conformation.

Self-organizing proteins are common in living matter and they are found in large aggregates for example in blood coagulation. Spherical like proteins are used in food industry as emulsifiers, gelling and foaming agents and in vitro they form Amyloid like structures. These latter fibers have properties (elasticity, solubility, etc) favorable for food texturing or to produce special structures. The milk protein beta-lactoglubulin studied by Mezzenga and his colleagues is at the beginning spherical and by a heat treatment accompanied by acid environment it aggregates into the filamentous structures. Beta-lactoglobulin is an important component of the milk serum and therefore very relevant for food industry.

The knowledge gained by the scientists on this food protein can potentially benefit medical sciences. In fact Amyloid-like fibers appear in humans affected by neurodegenerative diseases, like Alzheimer- or Creutzfeldt-Jakob disease. These human fibers, although made out of a very different proteins, are also ribbon-like and twisted and their assembly into long aggregates is presently under intense scrutiny. The model proposed by the team could also help to understand the genesis and development of theses diseases.

Giovanni Dietler | EurekAlert!
Further information:
http://www.epfl.ch

More articles from Life Sciences:

nachricht Closing the carbon loop
08.12.2016 | University of Pittsburgh

nachricht Newly discovered bacteria-binding protein in the intestine
08.12.2016 | University of Gothenburg

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Significantly more productivity in USP lasers

In recent years, lasers with ultrashort pulses (USP) down to the femtosecond range have become established on an industrial scale. They could advance some applications with the much-lauded “cold ablation” – if that meant they would then achieve more throughput. A new generation of process engineering that will address this issue in particular will be discussed at the “4th UKP Workshop – Ultrafast Laser Technology” in April 2017.

Even back in the 1990s, scientists were comparing materials processing with nanosecond, picosecond and femtosesecond pulses. The result was surprising:...

Im Focus: Shape matters when light meets atom

Mapping the interaction of a single atom with a single photon may inform design of quantum devices

Have you ever wondered how you see the world? Vision is about photons of light, which are packets of energy, interacting with the atoms or molecules in what...

Im Focus: Novel silicon etching technique crafts 3-D gradient refractive index micro-optics

A multi-institutional research collaboration has created a novel approach for fabricating three-dimensional micro-optics through the shape-defined formation of porous silicon (PSi), with broad impacts in integrated optoelectronics, imaging, and photovoltaics.

Working with colleagues at Stanford and The Dow Chemical Company, researchers at the University of Illinois at Urbana-Champaign fabricated 3-D birefringent...

Im Focus: Quantum Particles Form Droplets

In experiments with magnetic atoms conducted at extremely low temperatures, scientists have demonstrated a unique phase of matter: The atoms form a new type of quantum liquid or quantum droplet state. These so called quantum droplets may preserve their form in absence of external confinement because of quantum effects. The joint team of experimental physicists from Innsbruck and theoretical physicists from Hannover report on their findings in the journal Physical Review X.

“Our Quantum droplets are in the gas phase but they still drop like a rock,” explains experimental physicist Francesca Ferlaino when talking about the...

Im Focus: MADMAX: Max Planck Institute for Physics takes up axion research

The Max Planck Institute for Physics (MPP) is opening up a new research field. A workshop from November 21 - 22, 2016 will mark the start of activities for an innovative axion experiment. Axions are still only purely hypothetical particles. Their detection could solve two fundamental problems in particle physics: What dark matter consists of and why it has not yet been possible to directly observe a CP violation for the strong interaction.

The “MADMAX” project is the MPP’s commitment to axion research. Axions are so far only a theoretical prediction and are difficult to detect: on the one hand,...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

ICTM Conference 2017: Production technology for turbomachine manufacturing of the future

16.11.2016 | Event News

Innovation Day Laser Technology – Laser Additive Manufacturing

01.11.2016 | Event News

#IC2S2: When Social Science meets Computer Science - GESIS will host the IC2S2 conference 2017

14.10.2016 | Event News

 
Latest News

Closing the carbon loop

08.12.2016 | Life Sciences

Applicability of dynamic facilitation theory to binary hard disk systems

08.12.2016 | Physics and Astronomy

Scientists track chemical and structural evolution of catalytic nanoparticles in 3-D

08.12.2016 | Materials Sciences

VideoLinks
B2B-VideoLinks
More VideoLinks >>>