Protein biophysics PeerJ Award winner, Romina Gisonno, discusses biochemistry, amyloidosis, and her love of research
Well-deserved congratulations go to Romina Gisonno, winner of the PeerJ Award for Best Oral Presentation at the 4th Protein Biophysics at the end of the world. Held in Montevideo, Uruguay this past October, the meeting brought together computational and experimental researchers, undergraduate and graduate students from the areas of structural biology, bioinformatics, biochemistry, and biophysics.
The PeerJ Award includes a free publication in PeerJ – the Journal of Life and Environmental Sciences or one of our five PeerJ Chemistry journals (upon peer review and acceptance). Learn more about Romina’s research and award-winning presentation in her interview below.
Can you tell us a bit about yourself and your research interests?
I am a Biochemist and graduated from the National University of La Plata (UNLP) in 2016. I am currently in the third year of my PhD in Medical Sciences from the UNLP. I have a research grant provided by the same institution. In addition to my research assignments, I teach at the School of Medicine, which I enjoy very much.
The research group to which I belong, led by Drs. Nahuel Ramella and Alejandra Tricerri, is dedicated to the study of amyloidosis associated with apolipoptrotein A-I (apoA-I). My PhD project aims to inquire about the pathophysiology of this disease, particularly to study one of the natural variants of apoA-I that produces amyloidosis and atherosclerosis.
I enjoy research. I am a proactive person, always thinking about new projects and learning new techniques that allow me to train fully as a scientist. Once I finish my PhD, I intend to do internships or post-doctoral studies in other laboratories in the world to continue training and acquiring new skills.
Can you briefly explain the research you presented at PBATEOTW 2019?
The work I presented is part of my PhD project. It is entitled “Fibrillar conformation of an apolipoprotein A-I variant involved in amyloidosis and atherosclerosis.”
In this work, which describes relevant findings that are under consideration for publication, we were able to demonstrate that the conformation of apoA-I changes under oxidative conditions, tending to form aggregates, especially in the case of the natural variant Lys107-0. For the first time ever, we were able to form amyloid fibers of this deletion mutant that has been associated with severe atherosclerosis plus amyloidosis. Amyloid structures have been widely described for proteins such as α synuclein, the Aβa peptide, transthyretin, among others, but the existing apoA-I-linked information is fragmentary.
In addition, to characterize the aggregates formed under different conditions designed to study the role of oxidation, we demonstrate a divergent effect on the inflammatory response induced by the different conformations of apoA-I in the activation of human neutrophils.
From this work, we infer that a pro-inflammatory microenvironment could result in the formation of aggregation-prone species of apoA-I. These apoA-I aggregates would, in turn, induce a positive feedback in the activation of an inflammatory response.
This is an interesting study since it has high relevance in the field of atherosclerosis and will allow us to explain the close association between amyloidosis due to apoA-I Lys107-0 and severe atherosclerosis.
What are your next steps? How will you continue to build on this research?
Currently, I am performing cell biology assays that allow me to obtain more information about the pathophysiology of amyloidosis by apoA-I. In this way, I aim to establish a model closer to the molecular mechanisms that can occur in the body.
In addition, I continue to deepen the structural analysis of amyloid fibers by cryomicroscopy and other biophysical techniques.
In parallel with my laboratory work, I perform bioinformatics studies in collaboration with my partner, Molecular Biologist Tomás Masson. Currently, we are conducting studies on the evolution of apoA-I, whose results will allow us to understand the relationship between specific protein variants and their organ-specific pathology.
My goal is to be able to approach our unknowns from different points of view in order to have a more integrative knowledge of this pathology. Different experimental techniques are used to improve our understanding and accelerate the development of new therapeutic alternatives.
All this is possible thanks to the unconditional support of my directors Dr. Nahuel Ramella and Dr. Alejandra Tricerri to whom I thank for their support and trust.
I also greatly thank PeerJ for the opportunity to share my research.
For further enquiries about this project, you can contact me at: firstname.lastname@example.org
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PeerJ – the Journal of Life and Environmental Sciences is the peer-reviewed journal for Biology, Medicine and Environmental Sciences. PeerJ also publishes PeerJ Computer Science, and five newly launched PeerJ Chemistry journals.
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