title: P3 and P4 position analysis of vinyl ester pseudopeptide proteasome inhibitors.
abstract: Two small libraries of tripeptidic-based vinyl ester derivative proteasome inhibitors were synthesized and tested, starting with the Hmb-Val-Gln-Leu-VE prototype. The P3 and P4 positions were investigated with a complete set of amino acid residues, some of which showed remarkable selective inhibition of the trypsin-like (beta2) subunit. In both positions, aromatic and hydrophobic residues were preferred.
authors.affiliation: Department of Pharmaceutical Sciences and Biotechnology Center, University of Ferrara, I-44100 Ferrara, Italy. mru@dns.unife.it
authors.forename: Mauro
authors.initials: M
authors.lastname: Marastoni
authors.forename: Anna
authors.initials: A
authors.lastname: Baldisserotto
authors.forename: Claudio
authors.initials: C
authors.lastname: Trapella
authors.forename: Riccardo
authors.initials: R
authors.lastname: Gavioli
authors.forename: Roberto
authors.initials: R
authors.lastname: Tomatis
mesh_terms: D000595:Amino Acid Sequence; D004952:Esters / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D061988:Proteasome Inhibitors; D014753:Vinyl Compounds / Q000737:chemistry*
chemical_list: D004952:Esters; D010455:Peptides; D061988:Proteasome Inhibitors; D014753:Vinyl Compounds; D046988:Proteasome Endopeptidase Complex