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*

*この研究の対応する著者

研究成果: Article査読

16 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)3764-3769
ページ数6
ジャーナルAnalytical Chemistry
76
13
DOI
出版ステータスPublished - 2004 7 1
外部発表はい

ASJC Scopus subject areas

  • 分析化学

フィンガープリント

「Spontaneous integration of transmembrane peptides into a bacterial magnetic particle membrane and its application to display of useful proteins」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル