The triple helix is the hallmark protein structure of collagen. During tissue remodeling, the triple helical collagen molecules are degraded by specific proteases (e.g., MMP or cathepsin K) and become unfolded at body temperature. The Collagen Hybridizing Peptide (CHP) is a synthetic peptide that can specifically bind to such denatured collagen strands through hydrogen bonding, both in histology, in vivo, and in vitro (3D cell culture). By sharing the structural motif and the Gly-X-Y repeating sequence of natural collagen, CHP has a strong capability to hybridize with denatured collagen strands, in a fashion that is similar to a DNA fragment annealing to its complimentary DNA strand during PCR. CHP is an extremely specific probe for unfolded collagen molecules: it has negligible affinity to intact collagen molecules due to the lack of binding sites; it is also inert towards non-specific binding because of its neutral and hydrophilic nature.