Inhibition of Human and Yeast 20S Proteasome by Analogues of Trypsin Inhibitor SFTI-1
نویسندگان
چکیده
Starting from the primary structure of sunflower trypsin inhibitor SFTI-1, we designed novel non-covalent inhibitors of human and yeast 20S proteasomes. Peptides with Arg residue in P1 position and two basic amino acid residues (Lys or/and Arg) in P2' and P3' positions strongly inhibited chymotrypsin-like and caspase-like activities, while trypsin-like activity was poorly modified. We found that some SFTI-1 analogues up-regulated exclusively the chymotrypsin-like activity of latent yeast 20S proteasome.
منابع مشابه
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عنوان ژورنال:
دوره 9 شماره
صفحات -
تاریخ انتشار 2014