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Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates
Published on: December 6, 2017
Lipopolysaccaride-binding peptides obtained by phage display method
Megumi Matsumoto1, Yoshinobu Horiuchi, Akihiko Yamamoto
1Peptide Door Co. Ltd., Sangyo-sozo-kan 204, Shimonojo-machi 936-14, Takasaki, Gunma 370-0854, Japan.
Journal of Microbiological Methods
|April 24, 2010
Summary
New peptides were identified to bind lipopolysaccharide (LPS), a potent endotoxin. One peptide, Li5-001, shows high binding capacity for LPS, useful for pharmaceutical purification and diagnostics.
Area of Science:
- Microbiology
- Biochemistry
- Immunology
Background:
- Lipopolysaccharide (LPS) is a major endotoxin from Gram-negative bacteria.
- LPS toxicity can lead to sepsis and septic shock, necessitating early detection and neutralization.
- Current methods for LPS detection and removal have limitations.
Purpose of the Study:
- To discover and characterize novel LPS-binding peptides.
- To evaluate the binding affinity, capacity, and neutralizing activity of synthesized peptides.
- To assess the potential applications of these peptides in endotoxin removal and diagnostics.
Main Methods:
- Phage display was employed to identify LPS-binding peptides.
- Three selected peptides, including Li5-001, were synthesized.
- Binding affinity (K(d)) and capacity (ng LPS/mg) to LPS and lipid A were measured.
- LPS-neutralizing activity was assessed.
- The utility of Li5-001 coupled with beads was evaluated for endotoxin contamination removal and diagnostic assays.
Main Results:
- Several new LPS-binding peptides were obtained via phage display.
- Peptide Li5-001 demonstrated high binding affinity for LPS (K(d) = 10 nM) and lipid A (K(d) = 1 nM).
- Li5-001 exhibited a high binding capacity for LPS (130 ng LPS/mg), exceeding that of polymyxin B (80 ng LPS/mg).
- The LPS-neutralizing activity of Li5-001 was found to be low.
- Li5-001 coupled with beads showed potential for endotoxin removal and use in the Limulus amebocyte lysate test.
Conclusions:
- Peptide Li5-001 is a high-affinity, high-capacity LPS binder.
- Its properties make it suitable for removing endotoxin contamination from pharmaceuticals.
- The low neutralizing activity of Li5-001 allows its use in diagnostic assays like the Limulus amebocyte lysate test without LPS elution.
