In vitro selection of cathepsin E-activity-enhancing peptide aptamers at neutral pH

Madhu Biyani, Masae Futakami, Koichiro Kitamura, Tomoyo Kawakubo, Miho Suzuki, Kenji Yamamoto, Koichi Nishigaki

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

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 (KD; 300nM), 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.

Original languageEnglish
Article number834525
JournalInternational Journal of Peptides
Volume2011
DOIs
Publication statusPublished - 2011

All Science Journal Classification (ASJC) codes

  • Biochemistry

Fingerprint Dive into the research topics of 'In vitro selection of cathepsin E-activity-enhancing peptide aptamers at neutral pH'. Together they form a unique fingerprint.

Cite this