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  • Title: d-Amino Acid-Based Antifouling Peptides for the Construction of Electrochemical Biosensors Capable of Assaying Proteins in Serum with Enhanced Stability.
    Author: Zhao S, Qiao X, Chen M, Li Y, Wang X, Xu Z, Wu Y, Luo X.
    Journal: ACS Sens; 2022 Jun 24; 7(6):1740-1746. PubMed ID: 35616064.
    Abstract:
    The susceptibility of peptides to proteolytic degradation in human serum significantly hindered the potential application of peptide-based antifouling biosensors for long-term assaying of clinical samples. Herein, a robust antifouling biosensor with enhanced stability was constructed based on peptides composed of d-amino acids (d-peptide) with prominent proteolytic resistance. The electrode was electropolymerized with poly(3,4-ehtylenedioxythiophene) and electrodeposited with Au nanoparticles (AuNPs), and the d-peptide was then immobilized onto the AuNPs, and a typical antibody specific for immunoglobulin M (IgM) was immobilized. Because of the effect of d-amino acids, the d-peptide-modified electrode surface showed prominent antifouling capability and high tolerance to enzymatic hydrolysis. Moreover, the d-peptide-modified electrode exhibited much stronger long-term stability, as well as antifouling ability in human serum than the electrode modified with normal peptides. The electrochemical biosensor exhibited a sensitive response to IgM linearly within the range of 100 pg mL-1 to 1.0 μg mL-1 and a very low detection limit down to 37 pg mL-1, and it was able to detect IgM in human serum with good accuracy. This work provided a new strategy to develop robust peptide-based biosensors to resist the proteolytic degradation for practical application in complex clinical samples.
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