4.7 Article

An in vitro analysis of the hemostatic efficacy of fibrinogen precipitation with varied keratin fraction compositions

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DOI: 10.1016/j.ijbiomac.2023.125255

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Associated keratin proteins; Keratin intermediate filaments; Fibrinogen precipitation

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In preclinical studies, it has been found that human hair, containing keratin proteins, can be effectively used for hemostasis. However, due to the complex mixture and diverse molecular weights and structures of keratin proteins, their hemostatic capacity varies. To optimize the use of human hair keratin for hemostasis, the effects of different keratin fractions on fibrinogen precipitation were investigated. It was found that a mixture of high molecular weight keratin intermediate filaments (KIFs) and low molecular weight keratin-associated proteins (KAPs) in equal proportions yielded the most extensive precipitation of soluble fibrinogen. However, all hair protein samples showed different catalytic behaviors compared to thrombin, suggesting the potential of utilizing specific hair fractions to develop optimized hair protein-based hemostatic materials.
In preclinical studies, human hair has demonstrated effective hemostatic properties, potentially attributed to keratin proteins facilitating rapid conversion of fibrinogen to fibrin during coagulation. However, the rational use of human hair keratin for hemostasis remains unclear, given its complex mixture of proteins with diverse molecular weights and structures, leading to variable hemostatic capacity. To optimize the rational utilization of human hair keratin for hemostasis, we investigated the effects of different keratin fractions on keratin-mediated fibrinogen precipitation using a fibrin generation assay. Our study focused on high molecular weight keratin intermediate filaments (KIFs) and lower molecular weight keratin-associated proteins (KAPs) combined in various ratios during the fibrin generation. Scanning electron microscope analysis of the precipitates revealed a filamentous pattern with a broad distribution of fiber diameters, likely due to the diversity of keratin mixtures involved. An equal proportion of KIFs and KAPs in the mixture yielded the most extensive precipitation of soluble fibrinogen in an in vitro study, potentially due to structure-induced exposure of active sites. However, all hair protein samples exhibited diverse catalytic behaviors compared to thrombin, highlighting the potential of uti-lizing specific hair fractions to develop hair protein-based hemostatic materials with optimized capacity.

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