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Updated: Sep 26, 2026
Development and Validation of an Ultrasensitive Single Molecule Array Digital Enzyme-linked Immunosorbent Assay for Human Interferon-α
Published on: June 14, 2018
[Influence of the synthetic peptide recognized by neutralizing antibody on IFN-induced biological responses]
1National Laboratory of Molecular Virology and Genetic Engineering, Beijing 100052.
Objective:
The influence of synthetic peptide WLDPRH on IFN-induced biologic activity was studied.
Methods:
Based on our earlier studies in which two peptides were recognized by neutralizing antibody from the hexapeptide library displayed on the phage, one of the peptides synthesized, with amino acid sequence WLDPRH.
Results:
Computer-building approach showed that the synthetic peptide WLDPRH exhibited structural homology with LoopAB (29-35), the binding domain of type I IFN receptor. In the competitive ELISA studies, the synthetic peptide WLDPRH in 25 micrograms/ml could inhibit IFN binding neutralizing antibody 4C1. IFN-induced antiviral assay showed that the protective effects of suboptimal dose (20-70 pg/ml) of IFN were increased from 40% to 86% in the presence of the synthetic peptide WLDPRH and 1.4 micrograms/ml of the synthetic peptide WLDPRH was the lowest dose with the best protection. But potentiating effect on IFN-induced growth inhibition was fewer noticeable in 1.4 micrograms/ml of synthetic peptide.
Conclusion:
The results indicated that synthetic peptide WLDPRH can mimic the structure and activity of Loop AB in the IFN molecule and can be applied to immunotherapy as well as the mimic minimolecular design of IFN.
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