Lablog4-20:Screening of ACE-inhibitory peptides from a random peptide-displayed phage library using ACE-coupled liposomes

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Yoichi Kumada, Naoya Hashimoto, Fida MD Hasan, Masaaki Terashima, Kazuhiro Nakanishi, Alois Jungbauer, Shigeo Katoh

First author

Yoichi Kumada

Corresponding author

Shigeo Katoh

Publication Style

Journal name

Journal of biotechnology


Volume, issue, pages

131(2) 144-9


Angiotensin I converting enzyme (ACE)-inhibitory peptides were screened from a random peptide-displayed phage library using ACE-coupled liposomes. Among four kinds of inhibitory peptides selected by biopanning with two different elution strategies, a peptide (LSTLRSFCA) showed the highest inhibitory activity with an IC50 value of 3 μM. By measuring inhibitory activities of fragments of the peptide, it was found that the RSFCA region was a functional site to inhibit strongly the ACE catalytic activity, and particularly both Arg and Cys residues were essential for the strong inhibitory activity. The inhibitory activity of RRFCA was slightly increased, while that of the RSFRA, in which the Cys residue was replaced by Arg, was decreased to greater extent in comparison with the inhibitory activity of RSFCA. Taking into account the results obtained from the SPOT analysis, it was suggested that the Arg and Phe residues in RSFCA were important for a specific interaction with ACE, and the Cys residue inhibited the ACE activity. The cystein-based ACE-inhibitory peptides have not been isolated from processed food materials. These findings suggested that the biopanning method utilizing protein-coupled liposomes and random peptide librariesmight have a possibility to screen new functional peptides that are not found in processed food materials.