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

Analytical Chemistry
Tsuyoshi TanakaTadashi Matsunaga

Abstract

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 (R(12)), 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.

References

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Dec 24, 2002·The Journal of Biological Chemistry·Atsushi ArakakiTadashi Matsunaga

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Citations

Jun 19, 2008·Journal of the Royal Society, Interface·Atsushi ArakakiTadashi Matsunaga
Oct 28, 2008·Applied and Environmental Microbiology·Tsuyoshi TanakaTadashi Matsunaga
Jan 5, 2006·Applied and Environmental Microbiology·Tomoko Yoshino, Tadashi Matsunaga
Jul 1, 2009·Trends in Biotechnology·José Luis Corchero, Antonio Villaverde
Mar 16, 2013·Trends in Biotechnology·Samir GautamDavid A Spiegel
Oct 22, 2014·PloS One·Denis S GrouzdevKonstantin G Skryabin

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