Jorge Antonio Amador Balderas

I'm very happy to be attending #WATOC2025 this year in Oslo! I'll be presenting a poster of my work on DNA-Repair Enzymes on Tuesday! I'm super excited!

Which leads to some ligands binding differently to the metal, with some of them (like the best inhibitor) binding in a bidentate fashion, which would block the entrance of water to the binding site, leading to inhibition (4/4)

Also, Tyr or Phe doesn't make a critical difference in binding, as the enzyme prioritizes "filling" the hydrophobic pocket with the aromatic ring above other interactions. This also applies to ligands where Tyr and Phe had a D-configuration, with the Zn binding mode being the biggest difference(3/4)

Interestingly, there are no critical differences that allow us to distinguish between the binding of the inhibitors and the dipeptide, there is no clear trend where the molecules that are the best inhibitors to bind more or less tightly than the rest of the ligands (2/4)

Among other things, we analyzed the binding of the slowly hydrolyzed dipeptide Gly-Tyr/Phe; and inhibitors that are similar to the dipeptide (Tyr or Phe at the C-terminus and aminocarbonyl or hydroxyaminocarbonyl at the N-terminus) (1/4)

Mode of Metal Ligation Governs Inhibition of Carboxypeptidase A Carboxypeptidase is a Zn-dependent protease that specifically recognises and hydrolyses peptides with a hydrophobic side chain at the C-terminal residue. According to hydrolysis mechanisms proposed in...

I'm very happy to announce the publication of our work in Carboxypeptidase A; at the Computer Chemistry Center at @fau.de

www.mdpi.com/1422-0067/25...