Marcos Gil-Garcia

Will be recorded? I'm very interested! Thanks!

📣 @xabierjota.bsky.social and I are looking for candidates for a fully funded PhD position at UPV / EHU to study intrinsically disordered proteins using molecular simulations and computational chemistry calculations
👩‍🔬🧑‍🔬

📅 Deadline: October 1st

👇 Details below, please RT

Mont-Blanc massif from Le Lac Blanc.
Tour du Mont-Blanc 2025.

I am super excited to announce that I will be starting my lab at the Department of Pharmacology of the University of Zurich in Switzerland next year!

Crossover in Aromatic Amino Acid Interaction Strength: Tyrosine vs. Phenylalanine in Biomolecular Condensates Biomolecular condensates often form through the self-assembly of disordered proteins with low-complexity sequences. In these polypeptides, the aromatic amino acids phenylalanine and tyrosine act as ke...

Check out the updated version of our preprint "Crossover in Aromatic Amino Acid Interaction Strength: Tyrosine vs. Phenylalanine in Biomolecular Condensates", with @xabierjota.bsky.social
@dipcehu.bsky.social

www.biorxiv.org/content/10.1...

Biomolecular condensates as regulators of enzymatic reactions - Nature Chemical Engineering Open compartments, termed biomolecular condensates, are involved in cellular reactions. This Comment highlights their ability to enhance robustness and control of reactions in space and time, going be...

🚨Online now!

A Comment from Paolo Arosio & co-workers on biomolecular condensates as regulators of enzymatic reactions, with a look at how classical reaction engineering principles continue to provide insights into key underlying mechanisms. #ChemSky #ChemBio

www.nature.com/articles/s44... ($)

Biomolecular condensates as regulators of enzymatic reactions - Nature Chemical Engineering Open compartments, termed biomolecular condensates, are involved in cellular reactions. This Comment highlights their ability to enhance robustness and control of reactions in space and time, going be...

Glad to share our latest comment published in @natchemeng.nature.com
Here, we discuss the role of biomolecular condensates as regulators of enzymatic reactions.
I hope you enjoy it!
www.nature.com/articles/s44...

This pH buffering represents a possible function of biological enzymatic condensates and opens attractive applications of synthetic condensates in biocatalytic engineering and optimization of cascade reactions.

Enhancement of enzymatic activity by biomolecular condensates through pH buffering - Nature Communications Through local pH buffering, biomolecular condensates can expand the optimal pH interval for enzymatic reactions, increasing robustness to changes in solution pH and enabling network reactions with enz...

Glad to share our latest publication in @natcomms.nature.com!
Here, we show that pH buffering within the dense phase of condensates expands the pH interval which is optimal for enzymatic activity and enables optimization of one-pot cascade reactions.
www.nature.com/articles/s41...

This pipeline could represent a promising strategy for the rational design of interface-localizing peptides and the identification of the corresponding molecular grammar.

-This approach was validated by targeting 3 distinct condensates (hnRNPA1, Laf-1 and Ddx4 IDRs), observing that for the three cases, peptides display surfactant-like structures.
-The net charge of the scaffold is a key physicochemical parameter for designing these peptides.

De novo design of peptides localizing at the interface of biomolecular condensates The interface of biomolecular condensates has been shown to play an important role in processes such as protein aggregation and biochemical reactions. Targeted modulation of these interfaces could, th...

Glad to share our latest prepint!
-We developed a computational pipeline (combining CG simulations and ML) for the de novo design of peptides targeting condensate interfaces.
www.biorxiv.org/content/10.1...

De novo design of peptides localizing at the interface of biomolecular condensates https://www.biorxiv.org/content/10.1101/2025.05.09.653111v1

Monitoring neurodegeneration through brain-derived extracellular vesicles in biofluids The identification of neurodegenerative disease (ND) biomarkers in easily accessible body fluids is crucial in the fight against this class of disorde…

Happy to share our latest review/opinion on the role of BDEVs in neurodegeneration! We discuss their potential as a promising route for early diagnosis of NDs and the associated challenges and opportunities. Hope you enjoy it!
www.sciencedirect.com/science/arti...

Very interesting for an experimentalist working on biomolecular condensates! Congrats!!

Very nice talk! Congrats for such beautiful work!

Today @gogs-k.bsky.social, @tlhr.bsky.social, and I are launching @bindresearch.org, a UK-based not-for-profit research startup to deliver publicly–available tools and datasets to make intrinsically disordered proteins druggable. 🍝 💊🧲 💻 🦠

MIA40 circumvents the folding constraints imposed by TRIAP1 function. The MIA40 relay system mediates the import of small cysteine-rich proteins into the intermembrane mitochondrial space (IMS). MIA40 substrates are synt…

Here, we studied the structural duality of TRIAP1, where a redox-controlled structural transition resolves a folding kinetic trap by the assistance of the mitochondrial chaperone MIA40. (2/2)
www.sciencedirect.com/science/arti...

Back in time, I had the opportunity to work on studying the redox-controlled folding of small cysteine-rich proteins.

One intriguing example was TRIAP1. This small, disulfide-rich protein targets the IMS and plays a crucial role in phospholipid trafficking between mitochondrial membranes. (1/2)

Congratulations Xavier and team for such a beautiful work!