A Detailed Mapping of the Readily Accessible Disulfide Bonds in the Cortex of Wool Fibers
February 2021
in “
Proteins
”
disulfide bonds cysteine residues keratin intermediate filament proteins keratins keratin associated proteins KAPs reducing compounds N-terminal domains C-terminal domains head domains tail domains intermolecular bonds rod region crosslinking human epithelial keratins trichocyte intermediate filaments cysteine keratin reducing agents N-terminal C-terminal head tail human keratins hair filaments
TLDR Researchers found that the most reachable bonds in wool fibers are near the ends of certain proteins, which help stabilize the fiber's structure.
In the study from February 22, 2021, researchers investigated the accessibility of disulfide bonds within wool fibers, focusing on the interactions between cysteine residues in keratin intermediate filament proteins (keratins) and keratin associated proteins (KAPs). They built upon previous research by using reducing compounds to reveal a higher resolution of non-random cysteine interactions. The study found that the most accessible non-random cysteines in KAPs were located near the N- or C-terminal domains, while in keratins, they were present in the head or tail domains, suggesting their role in forming intermolecular bonds with KAPs. Less accessible non-random cysteines in keratins were found near or within the rod region, known for crosslinking in human epithelial keratins. This research provides insight into the specificity of disulfide bond interactions that stabilize fiber structure and highlights potential interaction sites between keratins and KAPs, as well as keratin-keratin interactions in trichocyte intermediate filaments.
