Description
Title: Applications for Regenerative Medicine Are Informed by Collagen Structure-Function Mapping
Abstract: The main protein in vertebrates, type I collagen, forms into fibrils that determine the shape and function of tissues like skin, tendons, and bones. Collagen functions abnormally to cause fibrosis, atherosclerosis, cancer metastasis, and brittle bone disease. Collagen also plays roles in hemostasis, wound healing, angiogenesis, and biomineralization. We created a type I collagen fibril interactome, which included its functional sites and disease-related mutations, to better understand the relationship between type I collagen structure and function. Whenever a model of X-ray diffraction of Data on the native collagen microfibril revealed a matrix interaction domain that performs structural functions like collagen assembly, crosslinking, proteoglycan (PG) binding, and mineralization, as well as a cell interaction domain supporting dynamic aspects of collagen biology like hemostasis, tissue remodeling, and cell adhesion. This model is confirmed by the type III collagen interactome. According to our hypothesis, the fibril displays a structural face in quiescent tissues, but tissue damage releases this face. he entry of blood into the collagenous stroma causes the cell and ligand binding sites on the fibrils to become exposed, which is essential for tissue remodeling and regeneration. Applications of our work include identifying anti-fibrotic antibodies, understanding how they interact with collagen, and drawing conclusions from our findings. The development of super-angiogenic collagens and collagen mimics is guided by angiogenesis studies and a collagen structure-function model.
Keywords: type I collagen; type III collagen; interactome; microfibril; ligand binding; extracellular matrix; connective tissue; fibrosis; angiogenesis; hemostasis; therapeutic antibodies
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Bioengineering
Writer Experience: 20+ Years
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