Collagen Structure Discovery: Biomedical Research Impact
- Houston — A team of scientists from Rice University and the University of Virginia (UVA) has uncovered a previously unknown collagen structure,potentially revolutionizing biomedical research.The study, led by...
- Published in ACS Central Science,the research details how advanced cryo-electron microscopy (cryo-EM) was used to visualize the atomic structure of a tightly packed collagen assembly.
- hartgerink, a professor of chemistry and bioengineering at Rice University, said the findings fundamentally change how scientists view collagen.
Scientists from Rice University adn UVA have made a groundbreaking discovery: a previously unknown collagen structure that could revolutionize biomedical research. This finding challenges existing assumptions about collagen’s structure using cryo-electron microscopy, revealing a deviation from the typical helical twist. This research broadens our understanding of collagen assemblies, impacting fields like regenerative medicine, wound healing, and drug delivery.This discovery has implications for various diseases involving compromised collagen. The study could lead to innovations in biomaterials and targeted therapies for collagen-related diseases. News Directory 3 is following this story closely to provide thorough coverage. Discover what’s next in collagen research and its impact!
Unexpected Collagen Structure Discovery Reshapes Biomedical Research
Updated feb. 7,2025
Houston — A team of scientists from Rice University and the University of Virginia (UVA) has uncovered a previously unknown collagen structure,potentially revolutionizing biomedical research.The study, led by Jeffrey Hartgerink and Tracy Yu at Rice, along with Mark Kreutzberger and Edward Egelman at UVA, challenges the long-held assumption that collagen, the body’s most abundant protein, has a predictable structure.
Published in ACS Central Science,the research details how advanced cryo-electron microscopy (cryo-EM) was used to visualize the atomic structure of a tightly packed collagen assembly. This structure deviates from the conventional right-handed superhelical twist, suggesting a greater structural diversity in collagen than previously recognized. This new understanding of collagen structure could lead to innovations in biomaterials.
hartgerink, a professor of chemistry and bioengineering at Rice University, said the findings fundamentally change how scientists view collagen. “For decades, we have assumed that collagen triple helices always follow a strict structural paradigm,” Hartgerink said. “Our findings show that collagen assemblies can adopt a wider range of conformations than previously thought.”
To investigate collagen assembly at the atomic level, the team created self-assembling peptides based on the collagen-like region of C1q, a key immune protein. Cryo-EM allowed them to analyze the structure of these assembled peptides in unprecedented detail, revealing the unexpected deviation from the standard superhelical twist. This unique conformation facilitates novel molecular interactions,including hydroxyproline stacking and the formation of a symmetrical hydrophobic cavity,indicating a broader structural diversity in collagen assemblies.
Yu, a former graduate student of hartgerink and current postdoctoral researcher at the University of Washington, noted the absence of the superhelical twist enables molecular interactions not previously observed in collagen.
Kreutzberger, the study’s first author, emphasized the discovery challenges existing beliefs about collagen structure and opens new avenues for exploring its biological roles. The discovery of this new collagen conformation has significance for medicine and biomaterials.
Collagen plays crucial roles in cell signaling, immune function, and tissue repair. A deeper understanding of its structural variability could provide new insights into diseases involving compromised collagen assembly,such as ehlers-Danlos syndrome,fibrosis,and certain cancers. Furthermore, this research could pave the way for creating novel materials for wound healing, tissue engineering, and drug delivery by leveraging the unique structural properties of the newly identified collagen conformation. The study highlights the importance of collagen’s role in tissue repair.
Egelman, a co-corresponding author of the study, said their research refines the understanding of collagen and underscores the need to re-examine other biological structures previously considered well understood.
What’s next
Future research will focus on exploring the implications of this newly discovered collagen structure for various biomedical applications, including regenerative medicine and the development of targeted therapies for collagen-related diseases.