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The Extracellular matrix proteins and soluble basic proteins category encompasses a wide array of structural and signaling molecules located in the interstitial space. Extracellular matrix (ECM) proteins, including collagen and fibronectin, provide the physical framework for tissues and modulate cell adhesion and migration [2]. Soluble basic proteins often include essential growth factors like Fibroblast Growth Factor (FGF) and Platelet-Derived Growth Factor (PDGF), which carry a positive charge at physiological pH [3]. These proteins are critical in regulating physiological processes such as wound healing, angiogenesis, and tissue remodeling. In pathological states like cancer, these proteins are often overexpressed or remodeled to support tumor growth and metastasis [1]. This broad group is targeted by polyanionic drugs, most notably suramin, which binds to the basic domains of these proteins via electrostatic interactions [1]. By sequestering these factors, such drugs prevent them from activating their respective cell-surface receptors, thereby inhibiting proliferative signaling. However, the lack of specificity inherent in targeting such a broad class of proteins leads to significant therapeutic challenges, including systemic toxicity and varied off-target effects.
Competitive inhibition of growth factor-receptor binding through electrostatic sequestration of basic protein domains by polyanionic compounds.
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