TY - JOUR
T1 - An in vitro analysis of the hemostatic efficacy of fibrinogen precipitation with varied keratin fraction compositions
AU - Chen, Wei Chieh
AU - Hsieh, Nien Chen
AU - Huang, Mao Cong
AU - Yang, Kai Chiang
AU - Yu, Jiashing
AU - Wei, Yang
N1 - Funding Information:
This study was supported by the Ministry of Science and Technology Research Program, MOST 108-2221-E-027-075- . Additionally, the authors are grateful for the financial support for this research by the University System of Taipei Joint Research Program under Grant No. USTP-NTUT-TMU-108-07 and USTP-NTUT-TMU-110-05 .
Publisher Copyright:
© 2023
PY - 2023/7
Y1 - 2023/7
N2 - 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 utilizing specific hair fractions to develop hair protein-based hemostatic materials with optimized capacity.
AB - 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 utilizing specific hair fractions to develop hair protein-based hemostatic materials with optimized capacity.
KW - Associated keratin proteins
KW - Fibrinogen precipitation
KW - Keratin intermediate filaments
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U2 - 10.1016/j.ijbiomac.2023.125255
DO - 10.1016/j.ijbiomac.2023.125255
M3 - Article
C2 - 37295701
AN - SCOPUS:85163100907
SN - 0141-8130
VL - 243
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
M1 - 125255
ER -