| 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]. |
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