Paige M F, Rainey J K, Goh M C
Department of Chemistry, University of Toronto, Ontario, Canada.
Biophys J. 1998 Jun;74(6):3211-6. doi: 10.1016/S0006-3495(98)78027-0.
Fibrous long spacing collagen (FLS) fibrils are collagen fibrils in which the periodicity is clearly greater than the 67-nm periodicity of native collagen. FLS fibrils were formed in vitro by the addition of alpha1-acid glycoprotein to an acidified solution of monomeric collagen and were imaged with atomic force microscopy. The fibrils formed were typically approximately 150 nm in diameter and had a distinct banding pattern with a 250-nm periodicity. At higher resolution, the mature FLS fibrils showed ultrastructure, both on the bands and in the interband region, which appears as protofibrils aligned along the main fibril axis. The alignment of protofibrils produced grooves along the main fibril, which were 2 nm deep and 20 nm in width. Examination of the tips of FLS fibrils suggests that they grow via the merging of protofibrils to the tip, followed by the entanglement and, ultimately, the tight packing of protofibrils. A comparison is made with native collagen in terms of structure and mechanism of assembly.
纤维状长间距胶原（FLS）原纤维是周期性明显大于天然胶原67纳米周期性的胶原原纤维。通过向酸化的单体胶原溶液中添加α1-酸性糖蛋白在体外形成FLS原纤维，并用原子力显微镜成像。形成的原纤维直径通常约为150纳米，具有250纳米周期性的明显条纹图案。在更高分辨率下，成熟的FLS原纤维在条带和条带间区域均显示出超微结构，表现为沿主原纤维轴排列的原纤维。原纤维的排列在主原纤维上产生了凹槽，这些凹槽深2纳米，宽20纳米。对FLS原纤维尖端的检查表明，它们通过原纤维合并到尖端，随后原纤维缠结并最终紧密堆积而生长。在组装结构和机制方面与天然胶原进行了比较。
