Publications
Catalina-Hernández È, López-Martín M, Masnou-Sánchez D, Martins MA, Lórenz‐Fonfría VA, Jiménez‐Altayó F, Hellmich UA, Inada H, Alcaraz A, Furutani Y, Nonell-Canals A, Vázquez-Ibar JL, Domene C, Gaudet R, Perálvarez‐Marín A (2023). Experimental and computational biophysics to identify vasodilator drugs targeted at TRPV2 using agonists based on the probenecid scaffold. CSBJ, 23, 473–482.
How do peptides interact with membranes?
Cell-Penetrating Peptides are small chains of amino acids that can cross biological membranes without causing damage to cells. Due to these unique properties, they possess interesting biomedical applications, such as vectors for drug delivery.
In our study, we computationally simulated the interaction of three of these peptides with model biological membranes to unravel the biophysical rules that govern these peptide-lipid interactions!
To read the full article, click here.
Catalina-Hernández, È., Aguilella-Arzo, M., Perálvarez-Marín, A., & López-Martín, M. (2025). Computational insights into membrane disruption by cell-penetrating peptides. Journal of Chemical Information and Modeling, 65(3), 1549–1559.
A new anti-hypertensive drug targeting TRPV2
Transient Potential Receptor (TRP) channels are a huge family of membrane proteins that are involved in a myriad of physiological processes such as sensing pain, temperature, different kinds of taste, pressure, and vision. They are also directly or indirectly related to multiple pathologies, such as cancer, bacterial infections, neurodegenerative disorders, obesity, or diabetes, among others.
One of these channels is TRPV2 (TRP subfamily Vanilloid), which has a crucial role in the function of cardiomyocytes. Although its role is so important, the pharmacology of this channel is scarce and rather non-specific.
In our study, we computationally screened 271 compounds and used a combination of computational and experimental tools to find a new drug (PSBA) that acts as a sex-biased vasodilator in rats!
To read the full article, click here.
Catalina-Hernández È, López-Martín M, Masnou-Sánchez D, Martins MA, Lórenz‐Fonfría VA, Jiménez‐Altayó F, Hellmich UA, Inada H, Alcaraz A, Furutani Y, Nonell-Canals A, Vázquez-Ibar JL, Domene C, Gaudet R, Perálvarez‐Marín A (2023). Experimental and computational biophysics to identify vasodilator drugs targeted at TRPV2 using agonists based on the probenecid scaffold. CSBJ, 23, 473–482.
Deciphering the virulence of an emerging, nosocomial pathogen
Bacterial resistance to antibiotics is a health problem that grows in importance and urgency year after year. Among the most problematic bacterial pathogens, the WHO puts Acinetobacter baumannii in the top of its Global Priority Pathogens List (https://www.who.int/publications/i/item/9789240093461).
Acinetobacter is an interesting bacterium. It mostly causes pneumonia in patients with assisted ventilation, but can also produce soft tissue and urinary tract infections, among others. It becomes resistant to antibiotics easily, survives long periods of time in desiccation conditions, and its mechanisms of virulence are largely unknown.
During my undergrad and my PhD I studied this problematic pathogen. In an early study during my undergrad laboratory placement, we characterized UmuDAb, a key gene involved in the SOS system, a response mechanism to DNA damage that allows this bacteria to survive environmental damaging agents (such as UV light) and acquire resistance to certain antibiotics.
To read the full article, click here.
In my PhD, I changed the focus: I studied how this bacterium regulates its virulence. During my project I characterized abaM, a gene coding for protein of unknown function. This gene is a central regulator of Quorum Sensing: a system used by many bacteria to communicate with each other via chemical signals. Mutating abaM totally disrupts this system, causing altered phenotypes in its motility, biofilm formation, gene expression, and virulence.
To read the full article, click here.
Are you REALLY interested? You can read my full thesis here.
Acinetobacter baumannii AB5075 motility on semi-solid agar (0.3%). The abaM mutant (right) has higher motility than the wild-type (left).