In Vitro Analysis of the Co-Assembly of Type-I and Type-III Collagen

被引:0
作者
Esma Eryilmaz
Winfried Teizer
Wonmuk Hwang
机构
[1] Texas A&M University,Department of Physics and Astronomy
[2] Selcuk University,Department of Biotechnology, College of Science
[3] Texas A&M University,Departments of Physics and Astronomy and Materials Science & Engineering
[4] Tohoku University,WPI Advanced Institute for Materials Research
[5] Texas A&M University,Department of Biomedical Engineering and Materials Science & Engineering
[6] Korea Institute for Advanced Study,School of Computational Sciences
来源
Cellular and Molecular Bioengineering | 2017年 / 10卷
关键词
AFM; Biomimetic surface; Collagen; Extracellular matrix; Heterogeneous assembly; Macromolecular assembly;
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摘要
An important step towards achieving functional diversity of biomimetic surfaces is to better understand the co-assembly of the extracellular matrix components. For this, we study type-I and type-III collagen, the two major collagen types in the extracellular matrix. By using atomic force microscopy, custom image analysis, and kinetic modeling, we study their homotypic and heterotypic assembly. We find that the growth rate and thickness of heterotypic fibrils decrease as the fraction of type-III collagen increases, but the fibril nucleation rate is maximal at an intermediate fraction of type-III. This is because the more hydrophobic type-I collagen nucleates fast and grows in both longitudinal and lateral directions, whereas more hydrophilic type-III limits lateral growth of fibrils, driving more monomers to nucleate additional fibrils. This demonstrates that subtle differences in physico-chemical properties of similar molecules can be used to fine-tune their assembly behavior.
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页码:41 / 53
页数:12
相关论文
共 194 条
[1]  
Birk DE(2001)Type V collagen: heterotypic type I/V collagen interactions in the regulation of fibril assembly Micron 32 223-237
[2]  
Birk DE(1997)Localization of collagen types I, III and V during tendon development. changes in collagen types I and III are correlated with changes in fibril diameter Eur. J. Cell Biol. 72 352-361
[3]  
Mayne R(1984)Collagen fibrillogenesis in vitro: comparison of types I, II, and III Arch. Biochem. Biophys. 235 178-185
[4]  
Birk DE(2007)Collagen fibrils: nanoscale ropes Biophys. J. 92 70-75
[5]  
Silver FH(2010)Suprastructures of extracellular matrices: paradigms of functions controlled by aggregates rather than molecules Cell Tissue Res. 339 7-18
[6]  
Bozec L(2001)Control of heterotypic fibril formation by collagen V is determined by chain stoichiometry J. Biol. Chem. 276 24352-24359
[7]  
van der Heijden G(2007)Creating ultrathin nanoscopic collagen matrices for biological and biotechnological applications Small 3 956-963
[8]  
Horton M(2006)Observing growth steps of collagen self-assembly by time-lapse high-resolution atomic force microscopy J. Struct. Biol. 154 232-245
[9]  
Bruckner P(2007)Temporal assembly of collagen type II studied by atomic force microscopy Adv. Eng. Mater. 9 1129-1133
[10]  
Chanut-Delalande H(2003)Thin films of collagen affect smooth muscle cell morphology Langmuir 19 1506-1514