Quartz crystal microbalance biosensor for recombinant human interferon-beta detection based on antisense peptide...

Area of Science:

• Biotechnology
• Biosensor Technology
• Biochemistry

Background:

• Recombinant human interferon-beta (rhIFN-beta) is a crucial therapeutic protein.
• Accurate and sensitive detection methods for rhIFN-beta are essential for research and clinical applications.
• Antisense peptides offer a potential platform for developing specific biosensors.

Purpose of the Study:

• To construct and evaluate quartz crystal microbalance (QCM) biosensors for rhIFN-beta detection.
• To investigate the impact of antisense peptide modification on binding affinity and biosensor performance.
• To demonstrate the feasibility of enhancing rhIFN-beta detection through optimized peptide design.

Main Methods:

• Immobilization of two antisense peptides (AS-1 and AS-2) onto QCM gold electrodes via a self-assembling monolayer.
• Evaluation of rhIFN-beta binding affinity using a QCM-flow injection analysis (QCM-FIA) system.
• Determination of dissociation constants (Kd) and assessment of biosensor precision, reproducibility, and linear response range.

Main Results:

• The modified antisense peptide (AS-2) exhibited a significantly higher binding affinity to rhIFN-beta compared to the original peptide (AS-1), with lower dissociation constants.
• Both biosensors demonstrated precise and reproducible detection of rhIFN-beta.
• A consistent linear response range (0.12-0.96 mg mL(-1)) was observed for rhIFN-beta binding to both biosensor types.

Conclusions:

• Highly selective QCM biosensors for rhIFN-beta were successfully constructed using the antisense peptide approach.
• Sequence modification of antisense peptides can effectively increase their binding affinity for target molecules.
• The developed biosensors show promise for sensitive and reliable detection of rhIFN-beta.