Please find below all relevant news regarding our Group.
Click on a headline in order to read the full article.

Our brand new review at Helvetica Chimica Acta is already available on-line

Happy to announce our last review concerning "Ruthenium Catalysis in Biological Habitats" is available through the journal website

We are very glad to share here that our review at Helv. Chim. Acta, entitled "Ruthenium Catalysis in Biological Habitats" and authored by A. Gutiérrez, F. López and J. L. Mascarenas, is already available through the journal website.

Abstract: Recent years have witnessed a considerable progress in research aimed at merging transition metal catalysis with chemical and cell biology. Therefore, a crescent number of metal-catalyzed transformations have been shown compatible with biological media and even with living settings. Of the different transition metals used to build these biocompatible catalysts, ruthenium has demonstrated to be particularly powerful, in part because the resulting complexes exhibit a very good balance between reactivity and biological stability. Indeed, ruthenium complexes have demonstrated utility to promote a great variety of reactions in biologically relevant contexts, from deprotection and redox processes to cycloadditions or photocatalytic transformations. Many of these reactions may enable the development of new type of biological tools and pharmacological strategies.

External link:

Our Commun. Chem. paper in collaboration with Prof. Vázquez, among others, has been selected as 2022 Editors’ Highlights

We are extremely happy to share the acknowledgement by Commun. Chem. editors', selecting our past year paper as one of the best for 2022

Editorial Board Member Professor Andy Wilson highlights Controlling oncogenic KRAS signaling pathways with a Palladium-responsive peptide by Eugenio Vázquez, José Mascareñas and colleagues ( “This is a really nice interdisciplinary manuscript at the interface of chemical biology and supramolecular chemistry; it is beautifully presented and focuses as its centrepiece on the ability to reversibly nucleate an α-helix through coordination of histidine residues placed at the i and i + 4 positions in the peptide sequence with cis-protected palladium. The method is applied to target a key protein–protein interaction that activates the MAP kinase pathway—the interaction between RAS and its activator SOS1. RAS frequently misfunctions in human cancers and has become an important target for development of molecular therapeutics. What is particularly impressive about the paper is the broad range of experiments used; both circular dichroism and NMR are used for structure elucidation of the stimuli responsive peptide, then direct fluorescence anisotropy binding and nucleotide exchange assays used to characterize interaction with RAS and inhibition of the SOS1/RAS interaction, and then finally cell uptake is monitored alongside effects on the MAPK kinase cascade through inhibition of ERK phosphorylation. A further important concept is introduced, specifically that whilst the palladium clip induces some helicity in the peptide, this is only partial, but the effect is proposed to be sufficient to promote RAS binding (relative to the peptide in the absence of palladium) through a bind and fold mechanism similar to that through which many intrinsically disordered proteins operate. Overall, the paper comprises rigorous experimentation and introduces several new concepts. Given the widespread interest in the development of constrained peptides as protein–protein interaction inhibitors, this represents an important advance for the area of constrained peptides.”

External link:

Our most recent collaboration is already on-line at Angew. Chem. Int. Ed.

So glad to announce our first 2023 paper and also collaborative work is already published on-line

We are very happy to share our Angew. Chem. Int. Ed. paper in collaboration with Jimenez-Osés research group has been accepted and it's already available through the journal website. This work is entitled "Iridium-Catalyzed ortho-Selective Borylation of Aromatic Amides Enabled by 5-Trifluoromethylated Bipyridine Ligands" and authored by D. Marcos-Atanes, C. Vidal, C. Navo, F. Pecatti, G. Jiménez-Osés and J. L. Mascareñas.

Abstract: Iridium-catalyzed borylations of aromatic C–H bonds are highly attractive transformations owing to the diversification possibilities offered by the resulting boronates. These transformations are best carried out using bidentate bipyridine or phenanthroline ligands, and tend to be governed by steric factors, therefore resulting in the competitive functionalization of meta and/or para positions. We have now discovered that a subtle change in the bipyridine ligand, namely, the introduction of a CF3 substituent at position 5, enables a complete alteration of regioselectivity in the borylation of aromatic amides, providing for the synthesis of a wide variety of ortho-borylated derivatives. Importantly, thorough computational studies suggest that the exquisite regio- and chemoselectivity stems from unusual outer-sphere interactions between the amide group of the substrate and the CF3–substituted aryl ring of the bipyridine ligand.

External link:

Goodbye Sara Gutiérrez

Sara Gutiérrez Hernández has left the group and she joined the Lilly pharma company. Good luck Sara!

Sara Gutiérrez Hernández has just left the group and she has joined the pharmaceutical Eli Lilly and Company, in Madrid (Spain), for a R&D-chemistry position.

Best of luck Sara!

Goodbye Xandro Vidal and Joan Miguel

Xandro Vidal Pereira and Joan Miguel Ávila have left the group to pursue their postdoctoral careers. Good luck to you both!

Xandro Vidal Pereira and Joan Miguel Ávila, two students that started at the group as CiQUS summer fellows and then went for their MSc and PhD also with us, have just left MetBioCat and they will pursue their postdoctoral careers.

Best of luck Xandro and Joan!

Goodbye Soraya Learte

Soraya Learte-Aymamí has left the group and she joined the Janssen pharma company. Good luck Soraya!

Soraya Learte-Aymamí has just left the group and she has joined the Janssen pharma company, in Spain, for a MSL position.

Best of luck Soraya!

Two in a row!! A second publication in collaboration with Prof. E. Vázquez is also on-line

Extremely happy to announce the second 2022 collaborative paper is already published

We are really glad to share this second 2022 collaborative paper, published at Commun. Chem., has been already accepted and it's available through the journal website. The communication is entitled "Controlling oncogenic KRAS signaling pathways with a Palladium-responsive peptide" and authored by S. Learte-Aymamí, P. Martin-Malpartida, L. Roldán-Martín, G. Sciortino, J. R. Couceiro, J.-D. Maréchal, M. J. Macias, J. L. Mascareñas and M. E. Vázquez.

Abstract: RAS oncoproteins are molecular switches associated with critical signaling pathways that regulate cell proliferation and differentiation. Mutations in the RAS family, mainly in the KRAS isoform, are responsible for some of the deadliest cancers, which has made this protein a major target in biomedical research. Here we demonstrate that a designed bis-histidine peptide derived from the αH helix of the cofactor SOS1 binds to KRAS with high affinity upon coordination to Pd(II). NMR spectroscopy and MD studies demonstrate that Pd(II) has a nucleating effect that facilitates the access to the bioactive α-helical conformation. The binding can be suppressed by an external metal chelator and recovered again by the addition of more Pd(II), making this system the first switchable KRAS binder, and demonstrates that folding-upon-binding mechanisms can operate in metal-nucleated peptides. In vitro experiments show that the metallopeptide can efficiently internalize into living cells and inhibit the MAPK kinase cascade.

External link:

Our most recent collaboration is already on-line at Chem. Commun.

So glad to announce our first 2022 collaborative paper is already published

We are very happy to share our Chem. Commun. paper in collaboration with Vázquez & Vázquez research group, among others, has been accepted and it's already available through the journal website. This work is entitled "Selective recognition of A/T-rich DNA 3-way junctions with a three-fold symmetric tripeptide" and authored by J. Gomez-Gonzalez, L. Martinez-Castro, J. Tolosa-Barrilero, A. Alcalde-Ordoñez, S. Learte-Aymamí, J. L. Mascareñas, J. C. García-Martínez, J. Martínez-Costas, J.-D. Maréchal, M. Vázquez and E. Vázquez.

Abstract: Non-canonical DNA structures, particularly 3-Way Junctions (3WJs) that are transiently formed during DNA replication, have recently emerged as promising chemotherapeutic targets. Here, we describe a new approach to target 3WJs that relies on the cooperative and sequence-selective recognition of A/T-rich duplex DNA branches by three AT-Hook peptides attached to a three-fold symmetric and fluorogenic 1,3,5-tristyrylbenzene core.

External link: