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Structural Study of a Peptide Epitope Bearing Multiple Post-Translational Modifications in Rheumatoid Arthritis.

María José Gómara1, Cristina García-Moreno1, Oriol Bárcenas2,3

  • 1Unit of Synthesis and Biomedical Applications of Peptides, IQAC-CSIC, Jordi Girona 18-26, 08034 Barcelona, Spain.

International Journal of Molecular Sciences
|September 27, 2025
PubMed
Summary
This summary is machine-generated.

Post-translational modifications (PTMs) in rheumatoid arthritis (RA) peptides alter their structure and autoantibody recognition. Different PTMs, like citrulline, influence binding, explaining autoantibody responses in RA patients.

Keywords:
AMPAsCDMDNMRPTMsRAconformationstructureα-fibrin (617–631) peptides

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Area of Science:

  • Biochemistry
  • Immunology
  • Structural Biology

Background:

  • Limited understanding of how post-translational modifications (PTMs) affect protein structure and antigen recognition.
  • Rheumatoid arthritis (RA) is associated with autoantibodies targeting citrullinated peptides.

Purpose of the Study:

  • To investigate the impact of RA-related PTMs on the conformation and autoantibody recognition of the α-fibrin (617-631) peptide.
  • To correlate structural changes induced by PTMs with autoantibody binding patterns in RA patients.

Main Methods:

  • Synthesis of ten peptides with varying numbers and types of PTMs (citrulline, homocitrulline, acetyl-lysine).
  • Analysis of peptide recognition by sera from RA patients.
  • Conformational analysis using circular dichroism (CD).
  • Structural determination via nuclear magnetic resonance (NMR) and enhanced-sampling molecular dynamics (MD) simulations.

Main Results:

  • Peptides with citrulline showed higher binding to anti-modified protein antibodies (AMPAs) compared to those with homocitrulline and/or acetyl-lysine.
  • The binding patterns varied depending on the PTM type and its position within the peptide sequence.
  • CD and NMR indicated half-turn conformations in the Lys620-Arg630 region.
  • MD simulations revealed that PTMs induce more collapsed conformations by altering intra-molecular interactions and hydrogen bonds.
  • Peptides with PTMs adopted different conformations than unmodified peptides, likely due to reduced net charge.

Conclusions:

  • PTMs significantly influence the conformation of the α-fibrin peptide antigen.
  • Structural alterations induced by PTMs affect autoantibody recognition in RA.
  • The specific type and position of PTMs dictate the conformational changes and subsequent autoantibody binding, offering insights into RA pathogenesis.