Abstract

Poster Presentations

Day 1, May 15（Wed.）　　Room P (Multi-purpose Hall)

1P-04　　PDF

A Novel Method for Mapping Protein-Protein Interaction by Capture of Biotinylated Peptide Using a Tamavidin, a Biotin-Binding Protein with Reversible Biotin-Binding Capability

(¹Kobe Univ., ²Kobe Univ., ³Kobe Univ., ⁴Kobe Pharm. Univ.)
^oKen-ichi Yoshino^1,2, Moeka Nishihara³, Shuji Ueda³, Atsuko Takeuchi⁴

Biotin-based labeling strategies such as BioID (proximity-dependent Biotin IDentification) and DiDBiT (Direct Detection of Biotin-containing Tag) are widely employed to study protein-protein interactions. While the high affinity of avidin for biotin greatly facilitates the capture of biotinylated proteins, it still presents a challenge for the recovery of biotinylated peptides. In the present study, we describe a Tamavidin-based biotinylated peptide capture strategy for mapping protein-protein interactions by liquid chromatography tandem mass spectrometry (LC/MS/MS). Tamavidins found in a Tamogitake mushroom are biotin-binding protein with reversible biotin-binding capability.