Developing exquisite collagen fibrillar assemblies in the presence of keratin nanoparticles for improved cellular affinity

Recently, the collagen-keratin (CK) composites have received much attention for the purpose of biomedical applications due to the intrinsic biocompatibility and biodegradability of these two proteins. However, few studies have reported the CK composites developed by the self-assembly approach and th...

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Bibliographic Details
Published in:International journal of biological macromolecules 2021-10, Vol.189, p.380-390
Main Authors: Ran, Yaqin, Su, Wen, Ma, Lei, Tan, Yunfei, Yi, Zeng, Li, Xudong
Format: Article
Language:English
Subjects:
Animals
Cattle
Cell Adhesion
Cell Death
Cell Movement
Cell Proliferation
Collagen
Cytocompatibility
Dynamic Light Scattering
Fibrillar Collagens - chemistry
Fibrillar Collagens - ultrastructure
Fibrillogenesis
Fibroblasts - cytology
Humans
Keratins - chemistry
Keratins - ultrastructure
Kinetics
Mice
Microscopy, Atomic Force
Nanoparticles
Nanoparticles - chemistry
Nanoparticles - ultrastructure
Nephelometry and Turbidimetry
NIH 3T3 Cells
Particle Size
Spectrophotometry, Ultraviolet
Spectroscopy, Fourier Transform Infrared
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Summary:Recently, the collagen-keratin (CK) composites have received much attention for the purpose of biomedical applications due to the intrinsic biocompatibility and biodegradability of these two proteins. However, few studies have reported the CK composites developed by the self-assembly approach and the influence of the keratin on the collagen self-assembly in vitro was still unknown. In this study, the keratin nanoparticles (KNPs) were successfully prepared by the reduction method, and we focused on investigating the effect of the varying concentrations of KNPs on the mechanism of the fibrillogenesis process of collagen. The intermolecular interaction between the two proteins revealed by the ultraviolet spectroscopy, Fourier transform-infrared (FT-IR) spectroscopy and circular dichromatic (CD) spectroscopy showed that KNPs would interact with the collagen, and keratin significantly influenced the hydrogen bonding interaction existed in collagen molecules. The SEM images exhibited the formation of exquisite fibrillar networks after incorporating the KNPs into collagen, and it was conspicuous that the KNPs could uniformly distribute on the surface of collagen fibrils via electrostatic interaction, for both of the two proteins possessed many charged moieties. In addition, the AFM images confirmed the presence of the characteristic D-periodicity of collagen fibrils, indicating that the introduction of KNPs did not disrupt the self-assembly nature of the native collagen. The cell adhesion, proliferation and migration experiments on the CK fibrils were also performed in this study. The results demonstrated that the CK composites showed a better cellular affinity compared with the collagen, thus it might be a promising candidate for the biomedical applications. [Display omitted] •The effect of keratin nanoparticles (KNPs) on the fibrillogenesis of type I collagen was dose-dependent.•The presence of KNPs possibly influenced the hydrogen bond interaction existing in collagen molecules.•The introduction of KNPs did not disrupt the self-assembly nature of native collagen.•The collagen-keratin (CK) composites exhibited the improved cellular affinity compared with collagen alone.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2021.08.134