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New Study Reveals Unexpected Collagen Structure
Context:
A groundbreaking study led by researchers from Rice University and the University of Virginia has unveiled an unexpected collagen structure that could revolutionise biomedical research.
More on News
- Published on February 3, 2025, in ACS Central Science, the study challenges long-held beliefs about collagen’s structural uniformity.
- Collagen, the most abundant protein in the human body, has traditionally been viewed as having a predictable, right-handed superhelical twist. However, the research team, led by Jeffrey Hartgerink and Tracy Yu, discovered a deviation from this canonical structure using advanced cryo-electron microscopy (cryo-EM).
Key Findings
- The collagen triple helix traditionally follows a right-handed superhelical twist. However, the study reveals that collagen can adopt more diverse forms than previously thought.
- Cryo-EM technology, which allows high-resolution imaging of biomolecules, provided unprecedented detail, revealing how this new conformation enables unique molecular interactions, including hydroxyproline stacking between adjacent helices.
- This stacking forms a symmetrical hydrophobic cavity, a feature not seen in the canonical structure.
Implications
- Biological Understanding: This discovery challenges existing dogma about collagen and may provide new insights into collagen’s biological roles, including its involvement in cell signalling, immune function, and tissue repair.
- Diseases and Disorders: The findings could lead to a better understanding of conditions where collagen assembly is disrupted, such as Ehlers-Danlos syndrome, fibrosis, and certain cancers.
- Biomedical Applications: The structural diversity of collagen could lead to advancements in biomaterials and regenerative medicine, offering the potential for new materials in wound healing, tissue engineering, and drug delivery.
