To achieve self-assembled collagen mimetic fibrils using designed peptides.
To achieve self-assembled collagen mimetic fibrils using designed peptides.
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作者：
Strawn R;Chen F;Jeet Haven P;Wong S;Park-Arias A;De Leeuw M;Xu Y
已经证明通过蛋白质设计获得胶原模拟原纤维具有挑战性。我们最近报道了使用设计的三重螺旋Col 108自组装显示35 nm，D-周期样，轴向重复结构的微纤维。肽Col 108通过使用合成基因的细菌表达制备;其三螺旋结构域由串联排列的三个假相同的氨基酸序列单元组成。据推测，Col 108微纤维的35 nm d-周期源自Col 108一级结构的周期性。相互交错的一个序列单元的相关的Col 108三重螺旋可以最大限度地提高螺旋间的相互作用，并产生所观察到的35 nm的d-周期。基于这种单元交错模型，预期仅由两个序列单元组成的三重螺旋具有形成相同d-周期性微原纤维的潜力。实际上，当制备这样的肽（肽2U 108）时，发现其自组装成具有35 nm的相同d-周期的微原纤维。相比之下，对于肽1U 108没有观察到d-周期性微原纤维，其在其一级结构中不具有长程重复序列。Col 108和2U 108的周期性微原纤维的发现表明了一种用于生物医学和工业应用的胶原蛋白模拟原纤维的方法。
It has proven challenging to obtain collagen-mimetic fibrils by protein design. We recently reported the self-assembly of a mini-fibril showing a 35 nm, D-period like, axially repeating structure using the designed triple helix Col108. Peptide Col108 was made by bacterial expression using a synthetic gene; its triple helix domain consists of three pseudo-identical units of amino acid sequence arranged in tandem. It was postulated that the 35 nm d-period of Col108 mini-fibrils originates from the periodicity of the Col108 primary structure. A mutual staggering of one sequence unit of the associating Col108 triple helices can maximize the inter-helical interactions and produce the observed 35 nm d-period. Based on this unit-staggered model, a triple helix consisting of only two sequence units is expected to have the potential to form the same d-periodic mini-fibrils. Indeed, when such a peptide, peptide 2U108, was made it was found to self-assemble into mini-fibrils having the same d-period of 35 nm. In contrast, no d-periodic mini-fibrils were observed for peptide 1U108, which does not have long-range repeating sequences in its primary structure. The findings of the periodic mini-fibrils of Col108 and 2U108 suggest a way forward to create collagen-mimetic fibrils for biomedical and industrial applications.
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