Design of the N-Terminus Substituted Curvature-Sensing Peptides That Exhibit Highly Sensitive Detection Ability of Bacterial Extracellular Vesicles


Posted: 2021-11-01 19:00:00
Chem Pharm Bull (Tokyo) . 2021;69(11):1075-1082. doi: 10.1248/cpb.c21-00516. Affiliations Expand Affiliations 1 Laboratory of Biofunctional Design Chemistry, Institute for Chemical Research, Kyoto University. 2 Laboratory of Molecular Microbial Science, Institute for Chemical Research, Kyoto University. Item in Clipboard Kenichi Kawano et al. Chem Pharm Bull (Tokyo). 2021. Show details Display options Display options Format Chem Pharm Bull (Tokyo) . 2021;69(11):1075-1082. doi: 10.1248/cpb.c21-00516. Affiliations 1 Laboratory of Biofunctional Design Chemistry, Institute for Chemical Research, Kyoto University. 2 Laboratory of Molecular Microbial Science, Institute for Chemical Research, Kyoto University. Item in Clipboard CiteDisplay options Display options Format Abstract Extracellular vesicles (EVs) have emerged as important targets in biological and medical studies because they are involved in diverse human diseases and bacterial pathogenesis. Although antibodies targeting the surface biomarkers are widely used to detect EVs, peptide-based curvature sensors are currently attracting an attention as a novel tool for marker-free EV detection techniques. We have previously created a curvature-sensing peptide, FAAV and applied it to develop a simple and rapid method for detection of bacterial EVs in cultured media. The method utilized the fluorescence/Förster resonance energy transfer (FRET) phenomenon to achieve the high sensitivity to changes in the EV amount. In the present study, to develop a practical and easy-to-use approach that can detect bacterial EVs by peptides alone, we designed novel curvature-sensing peptides, N-terminus-substituted FAAV (nFAAV) peptides. The nFAAV peptides exerted higher α-helix-stabilizing effects than FAAV upon binding to vesicles while maintaining a random coil structure in aqueous solution. One of the nFAAV peptides showed a superior binding affinity for bacterial EVs and detected changes in the EV amount with 5-fold higher sensitivity than FAAV even in the presence of the EV-secretory bacterial cells. We named nFAAV5, which exhibited the high ability to detect bacterial EVs, as an EV-sensing peptide. Our finding is that the coil-α-helix structural transition of the nFAAV peptides serve as a key structural factor for highly sensitive detection of bacterial EVs. Keywords: bacterial extracellular vesicle; coil–α-helix transition; dynamic conformation change; extracellular vesicle (EV)-sensing peptide; structure flexibility.

参考サイト PubMed: exsome



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