Impact of Ultrasonication on the Self-Assembly Behavior and Gel Properties of Bovine Bone Collagen I
文献类型： 外文期刊
作者： Liu, Hong 1 ; Zhang, Hongru 1 ; Wang, Kangyu 1 ; Qi, Liwei 1 ; Guo, Yujie 1 ; Zhang, Chunhui 1 ; Xu, Yang 3 ;
作者机构： 1.Chinese Acad Agr Sci, Inst Food Sci & Technol, Comprehens Key Lab Agroprod Proc, Minist Agr & Rural Affairs, Beijing 100193, Peoples R China
2.Univ Liege Gembloux Agrobio Tech, Lab Biomass & Green Technol, Passage Deportes 2, B-5030 Gembloux, Belgium
3.Inner Mongolia Mengtai Biol Engn Co Ltd, Hohhot 010000, Peoples R China
关键词： ultrasonic treatment; collagen fibril; self-assembly behavior; collagen fibril gel; gel property
期刊名称：MOLECULES （ 影响因子：4.6； 五年影响因子：4.9 ）
ISSN：
年卷期： 2023 年 28 卷 7 期
页码：
收录情况： SCI
摘要： This study deliberated the effect of ultrasonic treatment on collagen self-assembly behavior and collagen fibril gel properties. Bovine bone collagen I which had undergone ultrasonic treatment with different power (0-400 W) and duration (0-60 min) was analyzed. SDS-PAGE and spectroscopic analysis revealed that ultrasonic treatment decreased collagen molecular order degree and the number of hydrogen bonds, stretching collagen telopeptide regions while maintaining the integrity of the collagen triple-helical structure. Ultrasonic treatment (p <= 200 W, t <= 15 min) dispersed the collagen aggregates more evenly, and accelerated collagen self-assembly rate with a decreased but more homogeneous fibril diameter (82.78 +/- 16.47-115.52 +/- 19.51 nm) and D-periodicity lengths (62.1 +/- 2.9-66.5 +/- 1.8 nm) than that of the untreated collagen (119.15 +/- 27.89 nm; 66.5 +/- 1.8 nm). Meanwhile, ultrasonic treatment (p = 200 W, t <= 15 min) decreased the viscoelasticity index and gel strength, enhancing thermal stability and promoting specific surface area and porosity of collagen fibril gels than that of the untreated collagen fibril gel. These results testified that collagen self-assembly behavior and collagen fibril gel properties can be regulated by ultrasonic treatment through multi-hierarchical structural alteration. This study provided a new approach for controlling in vitro collagen fibrillogenesis process so as to manufacture novel desirable collagen-based biomaterials with propitious performances for further valorization.
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