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Mixed monolayer decorated SPR sensing surface for thrombin detection.

Demet Ataman Sadık1, İsmail Hakkı Boyacı2, Mehmet Mutlu3

  • 1Plasma Aided Bioengineering and Biotechnology (PABB) Research Group, Division of Nanotechnology and Nanomedicine, Institute of Natural and Applied Sciences, Hacettepe University, Ankara, Turkey.

Journal of Pharmaceutical and Biomedical Analysis
|August 28, 2019
PubMed
Summary

A novel surface plasmon resonance (SPR) immunosensor was developed for sensitive thrombin detection. The 3,3' Dithiodipropionic acid di (N-hydroxysuccinimide ester) (DSP):6-mercapto-1-hexanol (MCH) mixed self-assembled monolayer (mSAM) platform demonstrated excellent performance in detecting thrombin in complex matrices.

Keywords:
3,3′ Dithiodipropionic acid di (N-hydroxysuccinimide ester) DSP:6-mercapto-1-hexanol (MCH)Biological recognition element immobilizationBiosensorGold surfacesMixed self-assembled monolayers (mSAMs)Surface plasmon resonance (SPR)

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Area of Science:

  • Biosensing
  • Surface Chemistry
  • Biochemistry

Background:

  • Thrombin is a key biomarker in various physiological and pathological processes.
  • Accurate and sensitive detection of thrombin is crucial for clinical diagnostics.
  • Existing detection methods may lack sensitivity, specificity, or speed.

Purpose of the Study:

  • To develop and characterize a surface plasmon resonance (SPR) based immunosensor for the detection of thrombin.
  • To evaluate the performance of a novel mixed self-assembled monolayer (mSAM) interface for antibody immobilization.
  • To assess the immunosensor's sensitivity, selectivity, and applicability in complex biological samples.

Main Methods:

  • Fabrication of a mixed self-assembled monolayer (mSAM) using 3,3' Dithiodipropionic acid di (N-hydroxysuccinimide ester) (DSP) and 6-mercapto-1-hexanol (MCH) on a gold surface.
  • Immobilization of anti-thrombin antibody onto the mSAM surface.
  • Detection of varying concentrations of thrombin using flow cell coupled SPR.
  • Evaluation of selectivity against human serum albumin (HSA) and performance in diluted human serum samples.

Main Results:

  • The immunosensor exhibited a linear detection range of 30.0–100.0 nM for thrombin with a high R² value (0.992).
  • The Limit of Detection (LOD) and Limit of Quantification (LOQ) were determined to be 6.0 nM and 30.0 nM, respectively.
  • The immunosensor demonstrated high selectivity and effective thrombin detection in a diluted serum matrix, showing comparable performance to detection in PBS.

Conclusions:

  • The DSP:MCH mSAM interface is a highly promising platform for immobilizing biological recognition elements for biosensor development.
  • The developed SPR immunosensor offers a sensitive, selective, and robust method for thrombin detection.
  • This technology holds potential for applications in clinical diagnostics and biomedical research.