Scientists have actually discovered that collagen includes weak bonds that break under tension, protecting the rest of the tissue. Above is a collagen triple helix.
Recent findings about collagen, our bodys most abundant protein, reveal that its sacrificial bonds snap more quickly than the fundamental structure, therefore safeguarding the tissue as a whole– they locate hazardous radicals that are produced during mechanical tension.
One of the more unusual ways things can increase longevity is by compromising a part of themselves: This can vary from decoy burial chambers developed to mislead grave robbers, a fuse intentionally melting within an electrical circuit to secure other home appliances, or a lizards tail detaching to facilitate its escape.
This principle of sacrificial elements can also be observed in collagen, the most abundant protein in our bodies. Scientists at the Heidelberg Institute for Theoretical Studies (HITS) have actually exposed how the rupture of weak sacrificial bonds within collagen tissue helps to localize damage triggered by excessive force, reduce negative effect on the broader tissue, and promote healing.
Researchers have discovered that collagen includes weak bonds that break under stress, safeguarding the rest of the tissue.” Collagens impressive crosslink chemistry appears to be completely adapted to dealing with mechanical stress,” says Frauke Gräter, who led the research study at HITS. “By using complementary computational and speculative techniques to study collagen in rat tissue, our findings indicate that weak bonds within the crosslinks of collagen have a strong tendency to rupture before other bonds, such as those in the collagens foundation. Fully grown crosslinks in collagen consist of two arms: one of which is weaker than other bonds in collagen tissue. The scientists discovered that in regions of collagen tissue where weak bonds are present, other bonds– both in the crosslinks and the collagen backbone– are more likely to remain undamaged, therefore maintaining the structural stability of the collagen tissue.
Published in Nature Communications, the work shines light on collagens rupture systems, which is important for understanding tissue deterioration, product aging, and potentially advancing tissue engineering strategies.
” Collagens remarkable crosslink chemistry seems perfectly adapted to handling mechanical stress,” states Frauke Gräter, who led the research study at HITS. “By using complementary computational and experimental strategies to study collagen in rat tissue, our findings indicate that weak bonds within the crosslinks of collagen have a strong tendency to burst before other bonds, such as those in the collagens backbone. This functions as a protective system, localizes the harmful chemical and physical results of radicals triggered by ruptures, and most likely supports molecular healing processes.”
Collagen comprises approximately 30 percent of all proteins in the body. It supplies strength to bones, elasticity to skin, protection to organs, flexibility to tendons, aids in blood clotting, and supports the development of new cells. Structurally, collagen resembles a triple-braided helix: Three chains of amino acids intertwine to form a strong and stiff backbone.
Each collagen fiber contains countless individual molecules that are staggered and bound to each other by crosslinks, adding to collagens mechanical stability. It was thought that collagen crosslinks are susceptible to rupture, however little was known about the specific websites of bond ruptures or why ruptures happen where they do.
Scientists from the Molecular Biomechanics Group at HITS aimed to unravel these puzzles utilizing computer simulations of collagen across multiple biological scales and under different mechanical forces. By subjecting collagen to rigorous testing, the team was able to determine specific breakage points.
Mature crosslinks in collagen include 2 arms: one of which is weaker than other bonds in collagen tissue. When subjected to excessive force, the weaker arm is typically first to rupture, dissipating the force and localizing destructive impacts. The researchers discovered that in regions of collagen tissue where weak bonds exist, other bonds– both in the crosslinks and the collagen backbone– are more most likely to remain intact, thus maintaining the structural stability of the collagen tissue.
Previous work led by HITS researchers revealed that excessive mechanical stress on collagen causes the generation of radicals, which in turn trigger damage and oxidative stress in the body.
” Our latest research study shows that sacrificial bonds in collagen serve an important function in keeping the general integrity of the product can help to localize the effects of this mechanical tension that could otherwise have disastrous repercussions for the tissue,” describes Benedikt Rennekamp, the research studys very first author. “As collagen is a significant substituent of tissues in our bodies, by discovering and understanding these rupture sites, scientists can acquire important insights into the mechanics of collagen and possibly develop methods to enhance its strength and alleviate damage.”
Referral: “Collagen breaks at weak sacrificial bonds taming its mechanoradicals” by Benedikt Rennekamp, Christoph Karfusehr, Markus Kurth, Aysecan Ünal, Debora Monego, Kai Riedmiller, Ganna Gryn ova, David M. Hudson and Frauke Gräter, 12 April 2023, Nature Communications.DOI: 10.1038/ s41467-023-37726-z.
The study was funded by the H2020 European Research Council and Klaus Tschira Stiftung.
