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Tissue structural proteins are a diverse group of proteins that provide mechanical support, shape, and resilience to cells and tissues [1]. This category encompasses extracellular matrix (ECM) components like collagens, elastin, and laminins, as well as intracellular cytoskeletal proteins such as actin, tubulin, and intermediate filaments [1, 4]. These proteins are essential for maintaining tissue architecture, facilitating cell signaling through mechanotransduction, and enabling cell movement and division [4]. In various diseases, structural proteins are often dysregulated; for instance, excessive collagen deposition leads to organ fibrosis, while mutations in keratin or collagen genes cause hereditary skin and bone disorders [2, 4]. Pharmacologically, specific members of this group are significant targets; microtubule-targeting agents like taxanes and vinca alkaloids are widely used in oncology to disrupt mitosis, and collagen-modifying enzymes are used to treat fibroproliferative conditions [2, 3]. Because these proteins are ubiquitous throughout the body, therapeutic strategies must often balance efficacy with risks such as peripheral neuropathy or impaired wound healing [3].
Drugs targeting these proteins typically act by altering the polymerization dynamics of cytoskeletal elements (e.g., stabilizing or destabilizing microtubules) or by enzymatically degrading excessive extracellular matrix components to restore tissue flexibility [2, 3].
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