Collagen Mimetic Peptide with a Coiled Coil Trimerization Domain Forms Fibrils Having D-Period-like Structures.
Collagen Mimetic Peptide with a Coiled Coil Trimerization Domain Forms Fibrils Having D-Period-like Structures.
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具有卷曲螺旋三聚结构域的胶原模拟肽形成具有 D 周期样结构的原纤维。
DOI：
10.1021/acs.biomac.3c00901
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发表时间：
2023
影响因子：
6.2
通讯作者：
Xu,Yujia
中科院分区：
文献类型：
--
作者：
Dewan,Faizunnahar;Kirchner,Michele;Masoud,Fadi;Sami,Zainab;Xu,Yujia
纤维胶原是细胞外基质中的主要蛋白质，并通过化学和机械线索调节细胞行为。胶原原纤维的关键结构元素是由胶原三螺旋的侧向缔合形成的轴向重复D-周期。我们开发了具有重复氨基酸序列的原纤维形成胶原模拟肽（FCMPs），其形成具有D-周期样结构的原纤维。这些肽含有超过100个氨基酸残基，通过使用设计的基因的细菌表达产生。在这里，我们报告了含有α-螺旋卷曲结构域的新型FCMP的原纤维发生。最新的发现强调了氨基酸序列周期性在FCMP原纤维形成中的重要性。此外，我们的研究结果表明，胶原纤维的分子包装显着的适应性。这些FCMPs在结构和原纤维形成过程中都是天然胶原原纤维，是推进胶原研究和开发新型生物材料的有用分子工具。
Fibrillar collagen is the major protein in the extracellular matrix and regulates cell behavior via chemical and mechanical cues. The key structural element of collagen fibrils is the axially repeatingD-period, formed by the lateral association of collagen triple helices. We have developed fibril-forming collagen mimetic peptides (FCMPs) with repeated amino acid sequences, which form fibrils havingD-period-like structures. Containing over 100 amino acid residues, these peptides are produced by bacterial expression using designed genes. Here, we report the fibrillogenesis of a new FCMP containing an α-helix coiled coil domain. The latest findings highlight the importance of the amino acid sequence periodicity in FCMP fibril formation. Additionally, our results demonstrate the remarkable adaptability of collagen fibrils’ molecular packing. Mirroring native collagen fibrils, in both the structure and the fibrillogenesis process, these FCMPs are useful molecular tools for advancing collagen research and developing novel biomaterials.