胰蛋白酶抑制剂SFTI-1类似物对人和酵母20S蛋白酶体的抑制作用
Inhibition of human and yeast 20S proteasome by analogues of trypsin inhibitor SFTI-1.
作者信息
Dębowski Dawid, Pikuła Michał, Lubos Marta, Langa Paulina, Trzonkowski Piotr, Lesner Adam, Łęgowska Anna, Rolka Krzysztof
机构信息
Department of Bioorganic Chemistry, Faculty of Chemistry, University of Gdansk, Gdansk, Poland.
Department of Clinical Immunology and Transplantology, Medical University of Gdansk, Gdansk, Poland.
出版信息
PLoS One. 2014 Feb 25;9(2):e89465. doi: 10.1371/journal.pone.0089465. eCollection 2014.
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.
从向日葵胰蛋白酶抑制剂SFTI-1的一级结构出发，我们设计了新型的人源和酵母20S蛋白酶体非共价抑制剂。在P1位置含有精氨酸残基且在P2'和P3'位置含有两个碱性氨基酸残基（赖氨酸或/和精氨酸）的肽段能强烈抑制类胰凝乳蛋白酶和类半胱天冬酶活性，而类胰蛋白酶活性则很少被改变。我们发现一些SFTI-1类似物仅上调潜在酵母20S蛋白酶体的类胰凝乳蛋白酶活性。
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