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Denatured extracellular matrix (ECM) proteins in necrotic burn eschar are the primary pathological components of deep-thickness thermal injuries. Thermal trauma causes the irreversible denaturation and cross-linking of structural proteins, primarily collagen and elastin, resulting in a leathery, non-viable tissue layer known as eschar (StatPearls, 2023). This necrotic material serves as a reservoir for bacterial colonization and inhibits the natural wound-healing process by physically blocking the migration of keratinocytes and the formation of granulation tissue. Pharmacological targeting of these denatured proteins is achieved through enzymatic debridement, using agents like bromelain-enriched proteolytic enzymes or collagenases (FDA, 2022). These drugs selectively hydrolyze the damaged ECM components, facilitating the removal of the eschar while sparing the surrounding viable tissue. This process is critical for reducing the need for surgical excision, minimizing blood loss, and preparing the wound bed for definitive closure or grafting (PubMed, 2014).
Enzymatic debridement via selective proteolysis and hydrolysis of denatured collagen and elastin fibers within the necrotic tissue (FDA, 2022; Smith & Nephew, 2021).
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