Nucleation of Biomimetic Hydroxyapatite Nanoparticles on the Surface of Type I Collagen: Molecular Dynamics Investigations

2019 ◽  
Vol 123 (4) ◽  
pp. 2533-2543 ◽  
Author(s):  
Zhiyu Xue ◽  
Mingli Yang ◽  
Dingguo Xu
Keyword(s):  
Molecular Dynamics ◽  
Type I Collagen ◽  
Type I ◽  
Hydroxyapatite Nanoparticles ◽  
Biomimetic Hydroxyapatite

scholarly journals Contrasting Local and Macroscopic Effects of Collagen Hydroxylation

2021 ◽  
Vol 22 (16) ◽  
pp. 9068
Author(s):  
Sameer Varma ◽  
Joseph P. R. O. Orgel ◽  
Jay D. Schieber
Keyword(s):  
Molecular Dynamics ◽  
Hydrogen Bonding ◽  
Local Structure ◽  
Triple Helix ◽  
Type I Collagen ◽  
Chemical Change ◽  
Fibrillar Structure ◽  
Minor Effect ◽  
Type I ◽  
Macroscopic Properties

Collagen is heavily hydroxylated. Experiments show that proline hydroxylation is important to triple helix (monomer) stability, fibril assembly, and interaction of fibrils with other molecules. Nevertheless, experiments also show that even without hydroxylation, type I collagen does assemble into its native D-banded fibrillar structure. This raises two questions. Firstly, even though hydroxylation removal marginally affects macroscopic structure, how does such an extensive chemical change, which is expected to substantially reduce hydrogen bonding capacity, affect local structure? Secondly, how does such a chemical perturbation, which is expected to substantially decrease electrostatic attraction between monomers, affect collagen’s mechanical properties? To address these issues, we conduct a benchmarked molecular dynamics study of rat type I fibrils in the presence and absence of hydroxylation. Our simulations reproduce the experimental observation that hydroxylation removal has a minimal effect on collagen’s D-band length. We also find that the gap-overlap ratio, monomer width and monomer length are minimally affected. Surprisingly, we find that de-hydroxylation also has a minor effect on the fibril’s Young’s modulus, and elastic stress build up is also accompanied by tightening of triple-helix windings. In terms of local structure, de-hydroxylation does result in a substantial drop (23%) in inter-monomer hydrogen bonding. However, at the same time, the local structures and inter-monomer hydrogen bonding networks of non-hydroxylated amino acids are also affected. It seems that it is this intrinsic plasticity in inter-monomer interactions that preclude fibrils from undergoing any large changes in macroscopic properties. Nevertheless, changes in local structure can be expected to directly impact collagen’s interaction with extra-cellular matrix proteins. In general, this study highlights a key challenge in tissue engineering and medicine related to mapping collagen chemistry to macroscopic properties but suggests a path forward to address it using molecular dynamics simulations.

Specific osteogenesis imperfecta-related Gly substitutions in type I collagen induce distinct structural, mechanical, and dynamic characteristics

2021 ◽  
Author(s):  
Haoyuan Shi ◽  
Liming Zhao ◽  
Chenxi Zhai ◽  
Jingjie Yeo
Keyword(s):  
Molecular Dynamics ◽  
Hydrogen Bonds ◽  
Osteogenesis Imperfecta ◽  
Dynamic Characteristics ◽  
Type I Collagen ◽  
Type I ◽  
Vibrational Modes ◽  
Wild Type ◽  
Triple Helices ◽  
Dynamics Simulations

The stiffnesses, β-structures, hydrogen bonds, and vibrational modes of wild-type collagen triple helices are compared with osteogenesis imperfecta-related mutants using integrative structural and dynamic analysis via molecular dynamics simulations and...

scholarly journals Mechanical Properties of Type I Collagen: Insights From Molecular Dynamics Simulations

2011 ◽  
Vol 100 (3) ◽  
pp. 48a ◽  
Author(s):  
Paul Tumaneng ◽  
Guijun Zhao ◽  
Olga Antipova ◽  
Joseph P.R.O. Orgel ◽  
Sameer Varma ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Type I Collagen ◽  
Type I ◽  
Dynamics Simulations

Molecular Dynamics Exploration of Ordered-to-Disordered Surface Structures of Biomimetic Hydroxyapatite Nanoparticles

2018 ◽  
Vol 122 (12) ◽  
pp. 6691-6703 ◽  
Author(s):  
Qing Xie ◽  
Zhiyu Xue ◽  
Haojie Gu ◽  
Cuifang Hu ◽  
Mingli Yang ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Surface Structures ◽  
Hydroxyapatite Nanoparticles ◽  
Biomimetic Hydroxyapatite

Collagen fibrillogenesis in vitro: interaction of types I and V collagen

1986 ◽  
Vol 44 ◽  
pp. 210-211
Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk
Keyword(s):  
Type I Collagen ◽  
Corneal Stroma ◽  
Minor Component ◽  
Homogeneous Distribution ◽  
Type I ◽  
Type V Collagen ◽  
Fibril Morphology ◽  
Type V ◽  
In Vitro Interaction

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.

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