Spontaneous Integration of Transmembrane Peptides into a Bacterial Magnetic Particle Membrane and Its Application to Display of Useful Proteins

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 membr...

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Bibliographic Details
Published in:Analytical chemistry (Washington) 2004-07, Vol.76 (13), p.3764-3769
Main Authors: Tanaka, Tsuyoshi, Takeda, Hajime, Kokuryu, Yoriko, Matsunaga, Tadashi
Format: Article
Language:English
Subjects:
Analytical biochemistry: general aspects, technics, instrumentation
Analytical chemistry
Analytical, structural and metabolic biochemistry
Bacteria
Bacterial Proteins - chemistry
Biological and medical sciences
Biotin - chemistry
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Magnetics
Magnetism
Membrane Fusion
Membrane Proteins - chemistry
Membrane Proteins - physiology
Membranes
Membranes, Artificial
Peptide Fragments - chemical synthesis
Peptide Fragments - chemistry
Peptides
Peptides - chemical synthesis
Peptides - chemistry
Proteins
Sensitivity and Specificity
Sodium Chloride - chemistry
Streptavidin - chemistry
Surface Properties
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Summary: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.
ISSN:0003-2700
1520-6882
DOI:10.1021/ac035361m