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首页> 外文期刊>Biochemical and Biophysical Research Communications >Interactions between collagen IX and biglycan measured by atomic force microscopy.
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Interactions between collagen IX and biglycan measured by atomic force microscopy.

机译:通过原子力显微镜测量胶原蛋白IX和双糖链蛋白聚糖之间的相互作用。

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The stability of the lattice-like type II collagen architecture of articular cartilage is paramount to its optimal function. Such stability not only depends on the rigidity of collagen fibrils themselves, but more importantly, on their interconnections. One known interconnection is through type IX and biglycan molecules. However, the mechanical properties of this interaction and its role in the overall stability remain unrevealed. Using atomic force microscopy, this study directly measured the mechanical strength (or the rupture force) of a single bond between collagen IX and biglycan. The results demonstrated that the rupture force of this single bond was 15pN, which was significantly smaller than those of other known molecule interactions to date. This result suggested that type IX collagen and biglycan interaction may be the weak link in the cartilage collagen architecture, vulnerable to abnormal joint force and associated with disorders such as osteoarthritis.
机译:关节软骨的格状II型胶原结构的稳定性对其最佳功能至关重要。这种稳定性不仅取决于胶原纤维本身的刚度,而且更重要的是取决于它们的相互连接。一种已知的互连是通过IX型和双链聚糖分子。但是,这种相互作用的机械性能及其在整体稳定性中的作用仍未揭示。使用原子力显微镜,这项研究直接测量了胶原蛋白IX和双糖链蛋白聚糖之间单键的机械强度(或断裂力)。结果表明,该单键的断裂力为15pN,远小于迄今为止其他已知分子相互作用的断裂力。这一结果表明,IX型胶原蛋白和双糖链蛋白相互作用可能是软骨胶原蛋白结构中的薄弱环节,易受关节异常力的影响,并与骨关节炎等疾病有关。

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