Collagen Hybridizing Peptide, 5-FAM Conjugate (F-CHP)



Product Description


The collagen hybridizing peptide (CHP) is a novel and unique peptide that specifically binds unfolded collagen chains, both in vitro and in vivo.[1,2,3] By sharing the Gly-X-Y repeating sequence of natural collagen, CHP has a strong capability to hybridize with denatured collagen chains by reforming the triple helical structure, in a fashion similar to DNA fragments annealing to complementary DNA strands. CHP is extremely specific: it has negligible affinity to intact collagen molecules due to lack of binding sites, and it is inert towards non-specific binding because of its neutral and hydrophilic nature.

CHP is a powerful histopathology tool which enables straightforward detection of inflammation and tissue damage caused by a large variety of diseases, as well as tissue remodeling during development and aging.[3] CHP robustly visualizes the pericellular matrix turnover caused by proteolytic migration of cancer cells within 3D collagen culture, without the use of synthetic fluorogenic matrices or genetically modified cells.[4] CHP can measure and localize mechanical injury to collagenous tissue at the molecular level.[5] It also enables assessment of collagen denaturation in decellularized extracellular matrix.[6] In addition, CHP can be used to specifically visualize collagen bands in SDS-PAGE gels without the need for western blot.[7]

F-CHP is labeled with fluorescein for direct fluorescence detection.

Applications: immunofluorescence, cell imaging, SDS-PAGE (in-gel western)


Synonyms F-CHP, collagen mimetic peptide (CMP)
Molecular weight 2952.01 g/mol
Purity 95% by HPLC
Conjugate Single fluorescein tag per peptide
Excitation 494 nm
Emission 512 nm
Content Purified lyophilized powder
Storage -20 °C as powder, 4 °C after reconstitution in water



  • More informative, reliable and convenient than zymography, DQ collagen, SHG, and TEM
  • High affinity and unparalleled specificity to collagen with essentially no nonspecific binding
  • Applicable to all types of collagen from all species, relying on collagen's secondary structure instead of any defined sequence for binding
  • Suitable for both frozen and paraffin-embedded sections with no need for antigen retrieval
  • A non-antibody approach with no species restrictions against any co-staining antibody
  • Small size (2% of IgG by MW) enabling facile tissue penetration and whole specimen staining without sectioning
  • Stable in solution under 4 °C, eliminating the need to aliquot for storage 


Key Publications

  1. Targeting and mimicking collagens via triple helical peptide assemblies. Curr. Opin. Chem. Biol., 2013. [link]
  2. Targeting collagen strands by photo-triggered triple-helix hybridization. Proc. Natl. Acad. Sci. U.S.A., 2012. [link]
  3. In situ imaging of tissue remodeling with collagen hybridizing peptides. ACS Nano, 2017. [link]
  4. Visualizing collagen proteolysis by peptide hybridization: From 3D cell culture to in vivo imaging. Biomaterials, 2018. [link]
  5. Molecular level detection and localization of mechanical damage in collagen enabled by collagen hybridizing peptides. Nat. Commun., 2017. [link]
  6. Molecular assessment of collagen denaturation in decellularized tissues using the collagen hybridizing peptide. Acta Biomater., 2017. [link]
  7. Direct detection of collagenous proteins by fluorescently labeled collagen mimetic peptides. Bioconjug. Chem., 2013. [link]


Additional Information

CHP can slowly self-assemble into the triple helical structure in solution during storage. The trimeric CHP requires a simple heating step prior to usage. Please check the protocol for details: CHP_Datasheet.pdf

For research use only. Not intended or approved for diagnostic or therapeutic use.


Related Products

Collagen Hybridizing Peptide, Biotin Conjugate (B-CHP)


Product Citations

  1. Fiona Watt et al., Fibroblast state switching orchestrates dermal maturation and wound healing. bioRxiv (2018) more info
  2. Karl Kadler et al., Protection of circadian rhythms by the protein folding chaperone, BiP. bioRxiv (2018) more info
  3. Fiona Watt et al., Loxl2 is dispensable for dermal development, homeostasis and tumour stroma formation. Plos One (2018) more info
  4. Kenneth Monson et al., Detection and characterization of molecular-level collagen damage in overstretched cerebral arteries. Acta Biomaterialia (2018) more info
  5. Spencer Szczesny et al., Fatigue loading of tendon results in collagen kinking and denaturation but does not change local tissue mechanics. Journal of Biomechanics (2018) more info
  6. Samuel Veres et al., In tendons, differing physiological requirements lead to functionally distinct nanostructures. Scientific Reports (2018) more info
  7. Svenja Illien-Junger et al., Dietary advanced glycation end-product consumption leads to mechanical stiffening of murine intervertebral discs. bioRxiv (2018) more info
  8. Mark Banaszak Holl et al., Fatigue failure mechanism of anterior cruciate ligament fracture. (2018) more info
  9. Themis Kyriakides et al., Decellularized materials derived from TSP2-KO mice promote enhanced neovascularization and integration in diabetic wounds. Biomaterials (2018)