New research techniques that are born under the crossing of different disciplines
Find the intersection of the disciplines in the world of natural and exact sciences is no easy task. Find the interplay of knowledge and techniques that are managed from different perspectives, is not always accomplished successfully. However, and increasingly, the aim is to find an approach that combines edges that come from different worlds. It is like physics, chemistry, biology and mathematics itself, they are virtuously associated under a mixture that works as a valuable knowledge-producing machine.
An example of this, is the work that develops the Dr. J. Andrés Rivas Pardo, who belongs to the Department of Physics of the University of Santiago, working within the Soft Matter Research Center (SMAT-C). This Centre, is linked to a large group of scientists from from different areas of knowledge, all of them, gathered under the purpose of understanding the mechanical properties of different types of materials. Dr. Rivas Pardo has joined the Group of non-linear physics, where they engage in to study the mechanical processes that occur in nature, ranging from the locomotion of animals above about fluids, fractures of complex materials, and the elasticity of biomolecules such as DNA and proteins.
"I'm biochemist and did the PhD in molecular biology, in addition, did my postdoctoral training in Biophysics, in the latter, sought to understand the mechanical properties of elastic proteins using techniques of single molecules". This graphic the trans-disciplinarity that develops in the building where I work, which brings together professionals who come from the field of physics, chemistry and biology. It is a tridepartamental structure. A true intermodal complex", says the researcher.
The Pardo doctor Rivas trained in Enzymology with Dr. Emilio Cardemil from the University of Santiago. Subsequently, he migrated to the University of Chile, a place where he developed his doctoral thesis under the supervision of Dr. Victoria Guixé. In that instance, poured their efforts in the understanding of structural biology, combining innovative biophysical tools enzymology. In his postdoctoral fellow, received training in Biophysics of protein, mainly, in the understanding of mechanical processes associated with molecules involved in elastic functions. "The materials of the USC Center is deeply rooted to physics, discipline has much to do with the mecano-elasticos of protein processes. Under this scenario, the physics of polymers has advanced quickly, so my effort focused on acquiring knowledge about aspects such", says.
The researcher is being installed in the laboratory of Dr. Francisco Melo, also of the USACH and leader of the non-linear physics group, with the idea of understanding the processes involved in the systems elastic protein-protein interaction, but this time, at the level single molecule. "We use techniques of manipulation of molecules for applying calibrated forces and know their biophysical properties. And even though we have always understood the mechanical processes by applying force to proteins and DNA, in the laboratory we use two different techniques: magnetic tweezers and atomic force, both strategies are complementary and allow us to characterize biomolecules with different mechanical properties", explains.
The idea of this biochemist is to implement hybrid systems within the investigation of biomolecules, this means the registration of two different signals. "In our case we are trying to implement a system where we are able to disrupt an elastic protein in mechanical way and at the same time observing how it interacts with other proteins. We use a technique of transfer of energy known as FRET (Foster Resonance Energy Transfer), so that you can observe phenomena of fluorescence and mechanical processes at the same time. "Basically, we have two types of signals that converge to the same study, and are currently committed to applying this technique in the laboratory," he explains.
In that sense, researchers, through a new technology already implemetada in the laboratory can illuminate a specific molecule at a time. The technique called TIRF (Total Internal Reflection Fluorescence), generates a lighting from an evanescent field allowing to register a specific molecule, and not all the molecules contained in the sample. In this way, the work is much more specific. "We illuminate only the molecules that are specifically attached to the glass, which we got through the generation of an evanescent field where it enters an excitation light that matches the light absorption of the molecule, allowing this" flower, while the molecules that are just above them are not excited, since light does not penetrate into the middle. In this way, we only illuminate the first molecules that are attached to the glass. They are these same molecules which we later subjected to mechanical techniques or stretch,"explains the researcher.
In this way, the team that works the Pardo Dr. J. Andrés Rivas, has taken the first steps for the implementation of this new hybrid technique in the country, which expect can give interesting results in the study of proteins. Recently, Dr. Rivas Pardo has published article in the journal of the National Academy of Sciences of the United States, PNASimplementing a system that intervenes with newly synthesized proteins. "The technique is based on delivering a peptide that imitates structures already present in the protein of bacterial adhesion, so that this Mimetic peptide is incorporated into the normal protein folding. However, this peptide is like a small Trojan horse that binds to the protein hindering with folding and the elasticity of the molecule". While the published work is the proof of concept for the implementation of a system of anti-adhesion of bacteria, the idea is to continue the work with hybrid Instrumentation in the USACh SMAT-C Center. "We will combine mechanics with visualization of a molecule by means of TIRF-FRET, in order to generate a peptide-based strategy that can interfere with the adhesion of human pathogenic bacteria". Facing a traditional antibiotic, these peptides may have the advantage that the bacteria could not generate resistance without changing the way it uses its adhesion proteins, also a peptide Administration has many fewer complications for the individual to a common antibiotic.
Source: 4ID/CONGRESS, All rights reserved. ®
Journalist:Patricio Grunert Alarcón. ®
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