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Peer-reviewedCC BY 4.0ACS Omega

Molecular Engineering of Sarcosine Oxidase and Horseradish Peroxidase: Impact of Lysine Accessibility on Covalent Bioconjugation and Bioelectrocatalysis

  • Kamilė Ratkevičiu̅tė1
  • Simonas Grybas1
  • Ondrej Šedo2
  • Zbyněk Zdráhal2
  • Lidija Tetianec1
  • Gintautas Bagdžiu̅nas1
  1. 1Vilnius University , , Saulėtekio av. 7 , ,
  2. 2Masaryk University , , Kamenice 5 , ,
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Abstract

Sarcosine has emerged as a critical biomarker for the early diagnosis of prostate cancer, necessitating the development of highly sensitive and simplified electrochemical detection methods. While the bioconjugation of enzymes offers a pathway toward enhanced bioelectronic performance, biosensors based on bioconjugated sarcosine oxidase remain largely unexplored. In this study, we used a synthesized redox mediator, N-(ferrocenylmethyl)-6-aminohexanoic acid, featuring an extended spacer arm designed to decrease the tunneling distance between the enzyme cofactor and the electrode surface. Sarcosine oxidase and horseradish peroxidase were subjected to bioconjugation via carbodiimide-mediated coupling. The resulting bioconjugates were characterized by cyclic voltammetry, diffusion-kinetic analysis, and high-resolution mass spectrometry following tryptic and peptic digestion. Furthermore, an in silico structural analysis was employed to correlate lysine solvent-accessible surface area with conjugation efficiency. Based on these bioconjugates, a sarcosine biosensor was constructed and tested using human serum as real samples.

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Cite

BibTeXRIS
BibTeX
@article{ratkeviciute2026molecular,
  title = {{Molecular Engineering of Sarcosine Oxidase and Horseradish Peroxidase: Impact of Lysine Accessibility on Covalent Bioconjugation and Bioelectrocatalysis}},
  author = {Kamilė Ratkevičiu̅tė and Simonas Grybas and Ondrej Šedo and Zbyněk Zdráhal and Lidija Tetianec and Gintautas Bagdžiu̅nas},
  journal = {ACS Omega},
  year = {2026},
  month = nov,
  doi = {10.1021/acsomega.6c04756},
  url = {https://pubs.acs.org/acsodf/article/doi/10.1021/acsomega.6c04756/5463680/Molecular-Engineering-of-Sarcosine-Oxidase-and},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Molecular Engineering of Sarcosine Oxidase and Horseradish Peroxidase: Impact of Lysine Accessibility on Covalent Bioconjugation and Bioelectrocatalysis
AU  - Kamilė Ratkevičiu̅tė
AU  - Simonas Grybas
AU  - Ondrej Šedo
AU  - Zbyněk Zdráhal
AU  - Lidija Tetianec
AU  - Gintautas Bagdžiu̅nas
PY  - 2026
DA  - 2026/11/04
JO  - ACS Omega
DO  - 10.1021/acsomega.6c04756
UR  - https://pubs.acs.org/acsodf/article/doi/10.1021/acsomega.6c04756/5463680/Molecular-Engineering-of-Sarcosine-Oxidase-and
AB  - Sarcosine has emerged as a critical biomarker for the early diagnosis of prostate cancer, necessitating the development of highly sensitive and simplified electrochemical detection methods. While the bioconjugation of enzymes offers a pathway toward enhanced bioelectronic performance, biosensors based on bioconjugated sarcosine oxidase remain largely unexplored. In this study, we used a synthesized redox mediator, N-(ferrocenylmethyl)-6-aminohexanoic acid, featuring an extended spacer arm designed to decrease the tunneling distance between the enzyme cofactor and the electrode surface. Sarcosine oxidase and horseradish peroxidase were subjected to bioconjugation via carbodiimide-mediated coupling. The resulting bioconjugates were characterized by cyclic voltammetry, diffusion-kinetic analysis, and high-resolution mass spectrometry following tryptic and peptic digestion. Furthermore, an in silico structural analysis was employed to correlate lysine solvent-accessible surface area with conjugation efficiency. Based on these bioconjugates, a sarcosine biosensor was constructed and tested using human serum as real samples.
SN  - 2470-1343
ER  -