Open AccessIn Vitro Selection of Cathepsin E-Activity-Enhancing Peptide Aptamers at Neutral pH
Author(s) -
Madhu Biyani,
Masae Futakami,
Koichiro Kitamura,
Tomoyo Kawakubo,
Miho Suzuki,
Kenji Yamamoto,
Koichi Nishigaki
Publication year - 2011
Publication title -
international journal of peptides
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.239
H-Index - 25
eISSN - 1687-9775
pISSN - 1687-9767
DOI - 10.1155/2011/834525
Subject(s) - aptamer , cathepsin , peptide , protease , cathepsin d , cathepsin l , cathepsin e , cathepsin a , systematic evolution of ligands by exponential enrichment , cathepsin l1 , biology , biochemistry , in vitro , chemistry , microbiology and biotechnology , enzyme , cathepsin o , gene , rna
The aspartic protease cathepsin E has been shown to induce apoptosis in cancer cells under physiological conditions. Therefore, cathepsin E-activity-enhancing peptides functioning in the physiological pH range are valuable potential cancer therapeutic candidates. Here, we have used a general in vitro selection method (evolutionary rapid panning analysis system (eRAPANSY)), based on inverse substrate-function link (SF-link) selection to successfully identify cathepsin E-activity-enhancing peptide aptamers at neutral pH. A successive enrichment of peptide activators was attained in the course of selection. One such peptide activated cathepsin E up to 260%, had a high affinity (K D ; ∼ 300 nM), and had physiological activity as demonstrated by its apoptosis-inducing reaction in cancerous cells. This method is expected to be widely applicable for the identification of protease-activity-enhancing peptide aptamers.
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