Polypeptide semicarbazide glass slide microarrays: characterization and comparison with amine slides in serodetection studies

Bioconjug Chem. 2004 Mar-Apr;15(2):317-25. doi: 10.1021/bc034118r.

Abstract

We have described in the accompanying article the preparation of peptide-protein semicarbazide microarrays and their use for the simultaneous serodetection of antibodies directed against different pathogens. Here, we present a comparative study between semicarbazide and amine glass slides in an immunofluorescent serodetection assay using HIV (Gp120, Gp41), HCV (mix-HCV, core, NS3, and NS4), and HBV (HBs) recombinant antigens. Amine and semicarbazide surfaces displayed the same sensitivity for antibodies detection just after printing. However, the reactivity of protein antigens changed rapidly upon aging on amine slides but not on semicarbazide slides. Peptide or protein semicarbazide microarrays were found to be remarkably stable for months. Additional data concerning the characterization of the semicarbazide surface (homogeneity of the slides, chemical stability, contact angle measurements, atomic force microscopy studies, reproducibility of serodetection results) are also presented and discussed.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Validation Study

MeSH terms

  • Adsorption
  • Amines / chemistry*
  • Drug Stability
  • Glass / chemistry
  • Humans
  • Microscopy, Atomic Force
  • Peptides / chemistry*
  • Protein Array Analysis / instrumentation
  • Protein Array Analysis / methods*
  • Semicarbazides / chemistry*
  • Serologic Tests / instrumentation
  • Serologic Tests / methods*

Substances

  • Amines
  • Peptides
  • Semicarbazides