Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Controlling Protein Function With Nanotechnology

23.02.2012
A new study led by nanotechnology and biotechnology experts at Rensselaer Polytechnic Institute is providing important details on how proteins in our bodies interact with nanomaterials.
In their new study, published in the Feb. 2 online edition of the journal Nano Letters, the researchers developed a new tool to determine the orientation of proteins on different nanostructures. The discovery is a key step in the effort to control the orientation, structure, and function of proteins in the body using nanomaterials.

“To date, very little is known about how proteins interact with a surface at the nanoscale,” said Jonathan Dordick, director of the Center for Biotechnology and Interdisciplinary Studies at Rensselaer (CBIS), the Howard P. Isermann ’42 Professor of Chemical and Biological Engineering, and co-corresponding author of the study. “With a better understanding of how a protein interacts with a surface, we can develop custom nanoscale surfaces and design proteins that can do a variety of amazing tasks in the human body.”

Researchers seek to use nanotechnology in a variety of biological and medical applications, ranging from biosensors that can detect cancer in the body to scaffolds that help grow new tissues and organs, according to the researchers. Such technologies involve the interaction between biological cells and non-biological nanoscale materials. These interactions are controlled in part by proteins at the interface between the two materials. At such a minuscule level, the tiniest change in the structure of a material can vastly change the proteins involved and thus alter how the cells of the human body respond to the nanomaterial. In fact, proteins are among the most complex (and fickle) molecules in our bodies, rapidly changing their orientation or structure and thus their ability to interact with other molecules. Controlling their orientation and structure through their interactions with nanomaterials is essential to their reliable and safe use in new biotechnologies, according to Dordick.

“We have learned over the past decade to create nanomaterials with a wide variety of controlled structures, and we have discovered and begun to learn how these structures can positively impact cellular activity,” said Richard Siegel, the Robert W. Hunt Professor of Materials Science and Engineering at Rensselaer, director of the Rensselaer Nanotechnology Center, and co-corresponding author on the study. “By learning more about the role of the nanostructure-protein interactions that cause this impact, we will be able in the future to harness this knowledge to benefit society through improved healthcare. In addition to improved healthcare, this work will also help enable the manufacture of a wide range of new hierarchical composite materials—based upon synthetic polymers, biomolecules, and nanostructures—that will revolutionize our ability to solve many critical problems facing society worldwide.”

What the researchers found in this and their previous studies was that the size and curvature of the nanosurface greatly changed the way proteins oriented themselves on the surfaces and changed their structure, and this influenced protein stability. They found that nanostructures with smaller and more curved surfaces favored protein orientations that resulted in more stable proteins than structures with larger more flat surfaces.

To reach these conclusions, the researchers investigated several well-studied proteins, including cytochrome c, RNase A, and lysozyme and monitored their adsorption on different size silica nanoparticles. In this latest work, they chemically modified the adsorbed proteins to form chemical “tags” that provided the researchers with important information on how the proteins adsorbed on different silica surfaces. When the nanomaterials and proteins were studied using mass spectrometry, the tags provided valuable new information about the surface orientation of the proteins. Mass spectrometry analyzes the mass distribution of a material to determine its elemental composition and structural characteristics, and was very sensitive to the chemical tags added on the proteins.

Dordick and Siegel were joined in the research by Siddhartha Shrivastava and Joseph Nuffer of Rensselaer. The research was funded by the National Science Foundation. The paper is titled “Position-specific chemical modification and quantitative proteomics disclose protein orientation absorbed on silica nanoparticles.”

More information on Dordick’s research can be found at http://enzymes.che.rpi.edu/. Additional information on Siegel’s research can be found at http://www.rpi.edu/dept/nsec/.

Front and back face of Cytochrome C

Published February 22, 2012

Contact: Gabrielle DeMarco
Phone: (518) 276-6542
E-mail: demarg@rpi.edu

Gabrielle DeMarco | EurekAlert!
Further information:
http://www.rpi.edu

More articles from Life Sciences:

nachricht For a chimpanzee, one good turn deserves another
27.06.2017 | Max-Planck-Institut für Mathematik in den Naturwissenschaften (MPIMIS)

nachricht New method to rapidly map the 'social networks' of proteins
27.06.2017 | Salk Institute

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Can we see monkeys from space? Emerging technologies to map biodiversity

An international team of scientists has proposed a new multi-disciplinary approach in which an array of new technologies will allow us to map biodiversity and the risks that wildlife is facing at the scale of whole landscapes. The findings are published in Nature Ecology and Evolution. This international research is led by the Kunming Institute of Zoology from China, University of East Anglia, University of Leicester and the Leibniz Institute for Zoo and Wildlife Research.

Using a combination of satellite and ground data, the team proposes that it is now possible to map biodiversity with an accuracy that has not been previously...

Im Focus: Climate satellite: Tracking methane with robust laser technology

Heatwaves in the Arctic, longer periods of vegetation in Europe, severe floods in West Africa – starting in 2021, scientists want to explore the emissions of the greenhouse gas methane with the German-French satellite MERLIN. This is made possible by a new robust laser system of the Fraunhofer Institute for Laser Technology ILT in Aachen, which achieves unprecedented measurement accuracy.

Methane is primarily the result of the decomposition of organic matter. The gas has a 25 times greater warming potential than carbon dioxide, but is not as...

Im Focus: How protons move through a fuel cell

Hydrogen is regarded as the energy source of the future: It is produced with solar power and can be used to generate heat and electricity in fuel cells. Empa researchers have now succeeded in decoding the movement of hydrogen ions in crystals – a key step towards more efficient energy conversion in the hydrogen industry of tomorrow.

As charge carriers, electrons and ions play the leading role in electrochemical energy storage devices and converters such as batteries and fuel cells. Proton...

Im Focus: A unique data centre for cosmological simulations

Scientists from the Excellence Cluster Universe at the Ludwig-Maximilians-Universität Munich have establised "Cosmowebportal", a unique data centre for cosmological simulations located at the Leibniz Supercomputing Centre (LRZ) of the Bavarian Academy of Sciences. The complete results of a series of large hydrodynamical cosmological simulations are available, with data volumes typically exceeding several hundred terabytes. Scientists worldwide can interactively explore these complex simulations via a web interface and directly access the results.

With current telescopes, scientists can observe our Universe’s galaxies and galaxy clusters and their distribution along an invisible cosmic web. From the...

Im Focus: Scientists develop molecular thermometer for contactless measurement using infrared light

Temperature measurements possible even on the smallest scale / Molecular ruby for use in material sciences, biology, and medicine

Chemists at Johannes Gutenberg University Mainz (JGU) in cooperation with researchers of the German Federal Institute for Materials Research and Testing (BAM)...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

Plants are networkers

19.06.2017 | Event News

Digital Survival Training for Executives

13.06.2017 | Event News

Global Learning Council Summit 2017

13.06.2017 | Event News

 
Latest News

Touch Displays WAY-AX and WAY-DX by WayCon

27.06.2017 | Power and Electrical Engineering

Drones that drive

27.06.2017 | Information Technology

Ultra-compact phase modulators based on graphene plasmons

27.06.2017 | Physics and Astronomy

VideoLinks
B2B-VideoLinks
More VideoLinks >>>