Spontaneous integration of transmembrane peptides into a bacterial magnetic particle membrane and its application to display of useful proteins

Tsuyoshi Tanaka, Hajime Takeda, Yoriko Kokuryu, Tadashi Matsunaga

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An antimicrobial peptide, temporin L, and its derivative (TL-A2,) were employed as anchor peptides and displayed streptavidin on a bacterial magnetic particle (BMP) membrane. The ribotoxin L3 loop (L3) and the arginine-chain peptide (R12), which are carrier peptides permeable to eukaryotic cell membranes, were also used. The peptides were labeled with a fluorescent dye, 4-fluoro-7-nitrobenzofurazan (NBD), at the N-terminal region (NBD-peptides) and mixed with BMPs. A specific integration of NBD-temporin L into a BMP membrane was observed. The basic amino acids in temporin L played an important role in the integration into BMPs. Biotin conjugated to the N-terminus of temporin L was integrated into a BMP membrane. The C-terminus of temporin L was incorporated into a BMP membrane, and the N-terminus was located on the BMP membrane surface. The present study shows that temporin L is a stable molecular anchor on BMPs by the binding of soluble protein to the N-terminus.

Original languageEnglish
Pages (from-to)3764-3769
Number of pages6
JournalAnalytical Chemistry
Issue number13
Publication statusPublished - 2004 Jul 1
Externally publishedYes


ASJC Scopus subject areas

  • Analytical Chemistry

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