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Updated: Jun 7, 2026

Identification of Antibacterial Immunity Proteins in Escherichia coli using MALDI-TOF-TOF-MS/MS and Top-Down Proteomic Analysis
Published on: May 23, 2021
[SPR detection of affinity of antibacterial peptides in bactericidal/permeability-increasing protein domain for
Jing-qin Li1, Qing-li Kong, Zheng Fan
1Department of Laboratory Science, Yanjing Medical College, Beijing 101300, China.
Aim:
To study the affinity of endotoxin for three antibacterial peptides derived from N-terminal domain of bactericidal/permeability-increasing protein(BPI).
Methods:
To design and synthesize three peptides from N-terminal domain of BPI, BPI22-36, BPI85-99 and BPI147-161.Surface plasmon resonance(SPR) was used to monitor the interaction between LPS/lipid A and the peptides and polymyxin B(PMB) immobilized on CM5 sensor chip.
Results:
In three peptides, BPI147-161 was proved to have a best binding capacity with LPS/lipid A, followed by BPI85-99, but BPI22-36 could not interact with LPS/lipid A.The affinity constant K(A) of BPI147-161 with lipid A was 1.12 x 10⁶ L/mol. In contrast, the K(A) of PMB was 5.58 x 10⁶ L/mol.
Conclusion:
The results suggest that the peptide BPI147-161 from BPI effectively neutralize endotoxin and probably provide a novel treatment method for septic shock.
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