COLLAGEN STRUCTURE AND STABILITY

COLLAGEN STRUCTURE AND STABILITY

2009; 78: 929–958 | Matthew D. Shoulders and Ronald T. Raines
Collagen, the most abundant protein in animals, is composed of a right-handed bundle of three parallel, left-handed polyproline II-type helices. Recent studies have elucidated the structure and stability of collagen triple helices, highlighting the roles of stereoelectronic effects and preorganization. The fibrillar structure of type I collagen, the prototypical collagen fibril, has been detailed, and artificial collagen fibrils that exhibit some properties of natural collagen fibrils are now accessible through chemical synthesis and self-assembly. Understanding the mechanical and structural properties of native collagen fibrils will guide the development of artificial collagenous materials for biomedicine and nanotechnology. Key findings include the importance of interstrand hydrogen bonds, the impact of glycine substitutions, and the role of proline derivatives in stabilizing the triple helix. The stability of triple helices is influenced by stereoelectronic effects, steric effects, and n→π* interactions. Synthetic collagen heterotrimers and nonproline substitutions have also been explored, offering potential for biomaterial applications. The hierarchical structure of collagen fibrils, including microfibrils and fibrils, has been studied, and the mechanical properties of collagen monomers and fibrils have been measured. Research on collagenous biomaterials aims to develop materials that mimic the length, girth, patterns, mechanical properties, and complexity of natural collagen fibrils, with promising progress in recent years.Collagen, the most abundant protein in animals, is composed of a right-handed bundle of three parallel, left-handed polyproline II-type helices. Recent studies have elucidated the structure and stability of collagen triple helices, highlighting the roles of stereoelectronic effects and preorganization. The fibrillar structure of type I collagen, the prototypical collagen fibril, has been detailed, and artificial collagen fibrils that exhibit some properties of natural collagen fibrils are now accessible through chemical synthesis and self-assembly. Understanding the mechanical and structural properties of native collagen fibrils will guide the development of artificial collagenous materials for biomedicine and nanotechnology. Key findings include the importance of interstrand hydrogen bonds, the impact of glycine substitutions, and the role of proline derivatives in stabilizing the triple helix. The stability of triple helices is influenced by stereoelectronic effects, steric effects, and n→π* interactions. Synthetic collagen heterotrimers and nonproline substitutions have also been explored, offering potential for biomaterial applications. The hierarchical structure of collagen fibrils, including microfibrils and fibrils, has been studied, and the mechanical properties of collagen monomers and fibrils have been measured. Research on collagenous biomaterials aims to develop materials that mimic the length, girth, patterns, mechanical properties, and complexity of natural collagen fibrils, with promising progress in recent years.
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