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Debridement, the removal of diseased, nonviable tissue, is critical for clinicians to readily assess wound status and prepare the wound bed for advanced therapeutics or downstream active healing. Removing necrotic slough and eschar through surgical or mechanical methods is less specific and may be painful for patients. Enzymatic debridement agents, such as  Clostridial  collagenase, selectively and painlessly degrade devitalized tissue. In addition to its debriding activities, highly-purified  Clostridia l collagenase actively promotes healing, and our past studies reveal that extracellular matrices digested with this enzyme yield peptides that activate cellular migratory, proliferative and angiogenic responses to injury  in vitro , and promote wound closure  in vivo . Intriguingly, while collagenase Santyl ®  ointment, a sterile preparation containing  Clostridial  collagenases and other non-specific proteases, is a well-accepted enzymatic debridement agent, its role as an active healing entity has never been established. Based on our previous studies of pure  Clostridial  collagenase, we now ask whether the mixture of enzymes contained within Santyl ®  produces matrix-derived peptides that promote cellular injury responses  in vitro  and stimulate wound closure  in vivo . Here, we identify novel collagen fragments, along with collagen-associated peptides derived from thrombospondin-1, multimerin-1, fibronectin, TGFβ-induced protein ig-h3 and tenascin-C, generated from Santyl ®  collagenase-digested human dermal capillary endothelial and fibroblastic matrices, which increase cell proliferation and angiogenic remodeling  in vitro  by 50–100% over controls. Using an established model of impaired healing, we further demonstrate a specific dose of collagenase from Santyl ®  ointment, as well as the newly-identified and chemically-synthesized ECM-derived peptides significantly increase wound re-epithelialization by 60–100% over saline-treated controls. These results not only confirm and extend our earlier studies using purified collagenase- and matrix-derived peptides to stimulate healing  in vitro  and  in vivo , but these Santyl ® -generated, matrix-derived peptides may also represent exciting new opportunities for creating advanced wound healing therapies that are enabled by enzymatic debridement and potentially go beyond debridement.

plos one

Identification and Characterization of Novel Matrix-Derived Bioactive Peptides: A Role for Collagenase from Santyl® Ointment in Post-Debridement Wound Healing?