scholarly journals Hierarchical Structures, Formation Mechanism and Functional Properties of Collagen Fibrils(Part 1). Fine Structures of Mammalian Collagen Fibrils.

1994 ◽  
Vol 50 (5) ◽  
pp. 208-214
Author(s):  
Hajime Tsuchiya ◽  
Takashi Itoh ◽  
Takashi Konishi
2011 ◽  
Vol 21 (40) ◽  
pp. 16223 ◽  
Author(s):  
Yi Shi ◽  
Xiang Li ◽  
Junkai Hu ◽  
Jinhua Lu ◽  
Yuchun Ma ◽  
...  

2021 ◽  
Author(s):  
Pradipta Banerjee ◽  
Mayur Bajaj ◽  
Chetna Bhat ◽  
Y Geethika ◽  
Hemanth Irle

AbstractThis study had a two-fold objective: To utilize collagen hydrolysate for synthesizing a nanoscale Hydroxyapatite (HA) coating that would act as a superior osteoblast adhesion/proliferation agent compared to collagen-derived HA (C/HA) and to comprehend the significant role played by structural constraints on HA nucleation. Collagen was extracted from pacu skin with a high yield of 65.3% (w/w of tissue). It was digested by collagenase and the hydrolysate (CH) was purified with a high yield of 0.68g/g of collagen. The CH peptides had a mass of 6kDa, a predominant PP-II conformation and formed self-assembling hierarchical structures at physiological pH with dimensions of 842.2±229nm. The HA synthesized on CH (CH/HA) displayed higher yield when compared to C/HA. Structural analysis of CH/HA revealed that the PP-II peptides coiled to form mimic-helical moieties with reduced intermolecular packing distance of 0.9nm. The mimic helices cross-linked to form a vast quasi-fibrillar network that was comparatively smaller than collagen fibrils but exhibited enhanced stability and greater dynamicity. CH/HA displayed intense calcium-carboxyl interactions, sharper diffraction planes, smaller size of 48±6.2nm and a Ca/P ratio closer to 1.69 when compared to C/HA along with displaying serrated edge blooming crystals. Because of the small size, the CH/HA nanocrystals displayed significantly better osteoblast adhesion than C/HA and reduced the doubling time of cells. Overall, the results indicated that CH based nanocomposites displayed suitable morphological characteristics and cellular response for potential application as implant and bone graft coating material.Graphical abstract


RSC Advances ◽  
2017 ◽  
Vol 7 (1) ◽  
pp. 121-127 ◽  
Author(s):  
Muhammad Nawaz ◽  
Fangzhi Mou ◽  
Leilei Xu ◽  
Hao Tu ◽  
Jianguo Guan

Hydrothermal method was employed to prepare the flower-like hierarchical structures of F–Bi4TaO8Cl for photocatalytic hydrogen production under visible light irradiation.


2017 ◽  
Vol 36 ◽  
pp. 326-335 ◽  
Author(s):  
Oana Carp ◽  
Alina Tirsoaga ◽  
Ramona Ene ◽  
Adelina Ianculescu ◽  
Raluca F. Negrea ◽  
...  

2015 ◽  
Vol 2 (6) ◽  
pp. 567-575 ◽  
Author(s):  
Yong-Xia Zhao ◽  
Zhi-Wen Nie ◽  
Meng-Meng Shi ◽  
Cheng-Hui Zeng ◽  
Yuan Li ◽  
...  

Novel three-dimensional (3D) ceria hierarchical structures have been prepared via a thermolysis of the corresponding porous coordination polymer precursors.


CrystEngComm ◽  
2021 ◽  
Author(s):  
Ping Ou ◽  
Xuhong Su ◽  
Yang Zeng ◽  
Feifei Zhang ◽  
Jiahao Liu ◽  
...  

Two novel (NH4)xWO3 structures were prepared by a two-step hydrothermal route. Also, the possible formation mechanism of these two (NH4)xWO3 structures was proposed and discussed.


2012 ◽  
Vol 112 (3) ◽  
pp. 419-426 ◽  
Author(s):  
René B. Svensson ◽  
Philip Hansen ◽  
Tue Hassenkam ◽  
Bjarki T. Haraldsson ◽  
Per Aagaard ◽  
...  

Tendons are strong hierarchical structures, but how tensile forces are transmitted between different levels remains incompletely understood. Collagen fibrils are thought to be primary determinants of whole tendon properties, and therefore we hypothesized that the whole human patellar tendon and its distinct collagen fibrils would display similar mechanical properties. Human patellar tendons ( n = 5) were mechanically tested in vivo by ultrasonography. Biopsies were obtained from each tendon, and individual collagen fibrils were dissected and tested mechanically by atomic force microscopy. The Young's modulus was 2.0 ± 0.5 GPa, and the toe region reached 3.3 ± 1.9% strain in whole patellar tendons. Based on dry cross-sectional area, the Young's modulus of isolated collagen fibrils was 2.8 ± 0.3 GPa, and the toe region reached 0.86 ± 0.08% strain. The measured fibril modulus was insufficient to account for the modulus of the tendon in vivo when fibril content in the tendon was accounted for. Thus, our original hypothesis was not supported, although the in vitro fibril modulus corresponded well with reported in vitro tendon values. This correspondence together with the fibril modulus not being greater than that of tendon supports that fibrillar rather than interfibrillar properties govern the subfailure tendon response, making the fibrillar level a meaningful target of intervention. The lower modulus found in vitro suggests a possible adverse effect of removing the tissue from its natural environment. In addition to the primary work comparing the two hierarchical levels, we also verified the existence of viscoelastic behavior in isolated human collagen fibrils.


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