A groundbreaking study led by physics professor Nancy Forde and postdoctoral researcher Alaa Al-Shaer from Simon Fraser University has been published in the Proceedings of the National Academy of Sciences.

The research identifies key molecular features of collagen IV that contribute to its stability, helping to explain its crucial role in connective tissues despite its known structural instability at body temperature.

One of the significant findings is that cysteine amino acids in collagen IV can form bonds that act like 'staples' between strands, enhancing stability when heated and enabling better self-repair upon cooling.

In contrast, collagens lacking these cysteine bonds were found to be more prone to unraveling and unable to reassemble effectively after being heated.

The presence of these cysteine staples is not unique to humans; they are common across various species, indicating their significant functional role in collagen's stability throughout evolution.

This study is notable for being the first to utilize atomic force microscopy (AFM) to explore collagen stability across temperature changes, paving the way for future investigations into collagen-related diseases and aging processes.

The researchers emphasize the need for further research into mutated collagens associated with diseases, which could enhance our understanding of their mechanisms.

Forde and her team aim to investigate these mutated collagens to better understand their implications in diseases and aging.

Collagen is a vital protein, constituting about 20% of the proteins in the human body, and is essential for the structure and function of connective tissues such as tendons, bones, cartilage, and skin.

Despite its importance, collagen is known for its structural instability at body temperature, raising questions about how it maintains bodily integrity.

Using AFM, the team successfully visualized collagen proteins at various temperatures, revealing the intricate processes of how they unfold and refold.

Overall, this research sheds light on the molecular mechanisms that allow collagen to maintain its structure and function, which is critical for health and longevity.