0000000000851598
AUTHOR
Alex Perálvarez-marín
Design of novel small molecule base-pair recognizers of toxic CUG RNA transcripts characteristics of DM1.
Graphical abstract
Biophysical Characterization of TRPV2 Ion Channel
TRPV2 is a member of the superfamily of the Transient Receptor Potential (TRP) ion channels. These channels are assembled into homotetramers and allow cations across the membrane in response to physico-chemical stimuli such as heat, pressure, osmotic changes, etc. TRPV2 is an orphan receptor, since no specific endogenous ligand has been identified yet. To better understand the role of TRPV2 and to go further into its function, sequence analysis of orthologs for TRPV2 has been performed in order to define common and differential architectural regions. Preliminary biophysical characterization such as thermal stability, and secondary structure composition analysis has been carried out on the d…
Probing a Polar Cluster in the Retinal Binding Pocket of Bacteriorhodopsin by a Chemical Design Approach
Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C(13) of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoprotein…
Molecular and topological membrane folding determinants of transient receptor potential vanilloid 2 channel.
Transient Receptor Potential (TRP) channels are related to adaptation to the environment and somatosensation. The transient receptor potential vanilloid (TRPV) subfamily includes six closely evolutionary related ion channels sharing the same domain organization and tetrameric arrangement in the membrane. In this study we have characterized biochemically TRPV2 channel membrane protein folding and transmembrane (TM) architecture. Deleting the first N-terminal 74 residues preceding the ankyrin repeat domain (ARD) show a key role for this region in targeting the protein to the membrane. We have demonstrated the co-translational insertion of the membrane-embedded region of the TRPV2 and its disp…