ArticleScientific reports2026
Collagen hybridizing peptide to target in vivo misfolded collagen in OI zebrafish.
Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Osteogenesis imperfecta (OI) is a heritable connective tissue disorder characterized by defects in collagen I, leading to increased bone fragility and turnover. The zebrafish Chihuahua (Chi/+), carrying a p.(Gly736Asp) substitution in the α1(I) chain, recapitulates key features of human OI, including the presence of misfolded collagen I in extracellular matrix. In this study, we evaluated the specificity of a fluorescently labeled collagen hybridizing peptide (Cy5-CHP) for detecting in vivo misfolded collagen I in adult zebrafish. The CHP or the scrambled control peptides were injected intraperitoneally into WT and Chi/+ zebrafish, and average radiant efficiency was quantified at 24 and 72 h post-injection (hpi) in the vertebral column, cranium and heart, representing collagen I-rich organs, as well as the brain, a collagen I-poor tissue. Our results revealed Cy5-CHP specific binding to collagen I-rich tissues in Chi/+ zebrafish at 24 hpi, with minimal signal in the brain, whereas low signal was detectable across all tissues in WT. Cy5-CHP fluorescence was reduced by 72 hpi in all samples, consistent with the low binding affinity of the peptide. Histological analyses confirmed the co-localization of Cy5-CHP with collagen fibers in the endplates of Chi/+ vertebrae at 24 hpi. These findings provide the first in vivo evidence in zebrafish that Cy5-CHP selectively binds misfolded collagen, showing preferential accumulation in collagen I-rich tissues in OI. Overall, the results support the use of Cy5-CHP as a sensitive tool for detecting pathologic collagen and as a potential platform for tissue-targeted drug delivery in OI and other collagen-related disorders.
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