Collagen crosslinking

Collagen crosslinking refers to the formation of covalent bonds between collagen molecules in the extracellular matrix, a process essential for the mechanical strength and stability of connective tissues such as skin, tendons, and ligaments[1][2][3]. This modification is mediated by both enzymatic (primarily via lysyl oxidase and lysyl hydroxylase enzymes) and non-enzymatic (notably through the formation of advanced glycation end-products) mechanisms[1]. In skin and related structures, the peripheral, or perifollicular, region describes the area surrounding hair follicles, where collagen crosslinking is involved in maintaining dermal architecture and influencing tissue repair. Altered collagen crosslinking is implicated in a variety of pathological processes, such as fibrosis, aging, and metabolic disorders[1][2][3]. This process itself is not a single drug target but can be indirectly modulated through therapies that affect the enzymes or glycation reactions involved. Note on entry correctness: This is *not* a canonical molecular target (such as a receptor, protein, or enzyme). Rather, it is a post-translational *process* involving multiple molecules (e.g., collagen, lysyl oxidase, lysyl hydroxylase, AGEs). Therefore, it should not be listed as a standalone drug target or gene. Instead, if the intent is to identify druggable targets in this process, one should consider enzymes like **lysyl oxidase (LOX)**, **lysyl hydroxylase**, or the modification products themselves as potential targets[1][3].

Other names

Collagen cross-linkingCollagen crosslinks

Inhibition of enzymatic crosslinking through lysyl oxidase inhibition Inhibition of non-enzymatic glycation pathways