Enrichment of Collagen Fragments Using Dimeric Collagen Hybridizing Peptide for Urinary Collagenomics

Julian L. Kessler, Yang Li, Jaime Fornetti, Alana L. Welm, S. Michael Yu

Research output: Contribution to journalArticlepeer-review


Collagen remodeling in normal and pathologic conditions releases numerous collagen fragments into biological fluids. Although a few collagen fragments have been tested as biomarkers for disease indication, most occur at trace levels, making them nearly impossible to detect even with modern analytical tools. Here we report a new way to enrich collagen fragments that allows complete peptidomic analysis of collagen fragments in urine. Enrichment is made possible by dimeric collagen hybridizing peptides (CHPs) that bind collagen fragments originating from the triple helical regions of all collagen types with minimal sequence bias. LC-MS/MS analysis of enriched mouse urine revealed an average of 383 collagenous peptide fragments per sample (compared to 34 for unenriched sample), which could be mapped to all types of mouse collagens in the SwissProt database including FACITs and MACITs. Hierarchical clustering of a selected panel of the detected fragments separated osteopenic mice from healthy mice. The results demonstrate dimeric CHP's ability to enrich collagen fragments from biological fluid and its potential to aid peptidomics-based disease detection and biomarker discovery.

Original languageEnglish (US)
Pages (from-to)2926-2932
Number of pages7
JournalJournal of proteome research
Issue number8
StatePublished - Aug 7 2020


  • biomarkers
  • collagen hybridizing peptides
  • collagen remodeling
  • extracellular matrix

ASJC Scopus subject areas

  • General Chemistry
  • Biochemistry


Dive into the research topics of 'Enrichment of Collagen Fragments Using Dimeric Collagen Hybridizing Peptide for Urinary Collagenomics'. Together they form a unique fingerprint.

Cite this