Science Advances publishes the discovery of long-distance forces acting between proteins with a potential to sustain the high spatial organization and coordination of biomolecular reactions in cells.
Montpellier, France, February 16th, 2022 – Predicted since the beginning of the 20th century by classical and quantum electrodynamics, resonant electrodynamic intermolecular forces acting at a long distance had, up to now, eluded experimental detection. This is no longer the case as emerged from a collaborative work led by the teams of Marco Pettini of CPT/Aix-Marseille Univ./CNRS, Didier Marguet CIML/Inserm/CNRS /Aix Marseille Univ. and Jérémie Torrès of IES/Montpellier Univ.,/CNRS under the aegis of CNRS, and published in the prestigious scientific journal Science Advances (AAAS) under the title “Experimental evidence for long-distance electrodynamic intermolecular forces“. The peer-reviewed article reports an unprecedented experimental proof of principle of the activation of completely new forces acting between biomolecules and expanding above several hundreds of Angstroms. It opens a new domain of research aimed at exploring the mechanism contributing to the biomolecular high level of spatial organization and coordination for efficient transmission of information in cells and their functioning.
It all starts from one observation: what are the physical forces that bring the huge number of biochemical players in cells at the right place, in the right order and in a reasonably short time to sustain cellular function and ultimately cellular life? Biology has already demonstrated how, on short distance scales (less than ten Angstroms), well known forces (e.g. Coulomb, van der Waals, etc.) drive these intermolecular interactions and explain how proteins, when they get very close to each other, end up attracting and assembling together to start reactions. An importantquestion remaining open is: how do they get close enough to react? Are there other mechanisms beyond random “blind” movements that allow them to mutually “find each other” when and where needed?
The research paper published in Science Advances presents the discovery of completely new electrodynamic forces acting between biomolecules and extending beyond several hundreds or even thousands of Angstroms, opening up a new representation of protein interaction mechanisms. Revealed through an original experimental technique based on terahertz spectroscopy in solution and fluorescence correlation spectroscopy, and corroborated by theoretical calculations, the authors have shown that the activation of long-range forces only occurs when the molecules are driven out of thermal equilibrium. This discovery sheds new light on the recruitment of biomolecular reaction partners over long distances.
In perspective, these early results could contribute to the development of much-needed new personalized drugs/medicines and to the discovery of therapies, particularly in the field of immunotherapy. They also might contribute to the developing field of optogenetics and constitute a key to better understand the mechanisms of interaction between electromagnetic fields and living matter. Prof. Marco Pettini, Aix-Marseille Univ. “This experimental discovery is of fundamental physical
relevance as it will require extending the list of known intermolecular interactions commonly described in scientific textbooks, moreover this result could bring to paradigm shifting in biophysics. “The project leading to this publication has received funding from the Excellence Initiative of Aix-Marseille University (A*MIDEX) under the project MOLINT led by Prof. Marco Pettini, and from the European Commission (2021-2024) under the EU Project LINkS that is currently being conducted by Pr. Jérémie Torrès ( https://project-links.eu/ ).
The published article can be found on Science Advances’ website and in a downloadable version by clicking on this link: sciadv.LINkS.