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. CHP can measure and localize mechanical injury to collagenous tissue at the molecular level. It also enables assessment of collagen denaturation in decellularized extracellular matrix. In addition, CHP can be used to specifically visualize collagen bands in SDS-PAGE gels without the need for western blot.
B-CHP is labeled with biotin for avidin/streptavidin-mediated detection. B-CHP offers flexible detection options, such as non-green fluorescence and HRP-enzyme methods, to avoid background and enhance signal.
Applications: immunofluorescence, immunohistochemistry
|Synonyms||B-CHP, collagen mimetic peptide (CMP)|
|Molecular weight||2762.01 g/mol|
|Purity||95% by HPLC|
|Conjugate||Single biotin tag per peptide|
|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
B-CHP provides the flexibility for visualizing damaged collagen using any user-selected fluorophore (e.g., AlexaFluor dyes conjugated streptavidin), or a non-fluorescence method (e.g., through NeutrAvidin-HRP mediated DAB staining).
In addition, B-CHP and commercial streptavidin-conjugated gold nanoparticles can be used in combination to label unfolded collagen molecules under TEM: collagen fibers in an intact or mechanically overloaded rat tail tendon probed by B-CHP and streptavidin conjugated 10nm-sized gold nanoparticles (scale bar: 200 nm).
- Targeting and mimicking collagens via triple helical peptide assemblies. Curr. Opin. Chem. Biol., 2013. [link]
- Targeting collagen strands by photo-triggered triple-helix hybridization. Proc. Natl. Acad. Sci. U.S.A., 2012. [link]
- In situ imaging of tissue remodeling with collagen hybridizing peptides. ACS Nano, 2017. [link]
- Molecular level detection and localization of mechanical damage in collagen enabled by collagen hybridizing peptides. Nat. Commun., 2017. [link]
- Molecular assessment of collagen denaturation in decellularized tissues using the collagen hybridizing peptide. Acta Biomater., 2017. [link]
- Direct detection of collagenous proteins by fluorescently labeled collagen mimetic peptides. Bioconjug. Chem., 2013. [link]
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.