The origin of the triple‐helix structure and high stability of collagen has been debated for many years. As models of the triple helix and building blocks for new biomaterials, collagen mimetic peptide (CMP) assemblies have been deeply studied in the condensed phase. In particular, it was found that hydroxylation of proline, an abundant post‐translational modification in collagen, increases its stability. Two main hypotheses emerged to account for this behavior: 1) intra‐helix stereoelectronic effects, and 2) the role of water molecules H‐bound to hydroxyproline side‐chains. However, in condensed‐phase investigations, the influence of water cannot be fully removed. Therefore, we employed a combination of tandem ion mobility and mass spectrometries to assess the structure and stability of CMP assemblies in the gas phase. These results show a conservation of the structure and stability properties of triple helix models in the absence of solvent, supporting an important role of stereoelectronic effects. Moreover, evidence that small triple helix assemblies with controlled stoichiometry can be studied in the gas phase is given, which opens new perspectives in the understanding of the first steps of collagen fiber growth.

中文翻译：

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分离的胶原模拟肽装配体具有稳定的三螺旋结构

三螺旋结构的起源和胶原的高稳定性已经争论了很多年。作为新型生物材料的三重螺旋模型和构造单元，在缩合阶段已对胶原蛋白模拟肽（CMP）组件进行了深入研究。特别是，发现脯氨酸的羟基化是胶原蛋白中大量的翻译后修饰，可增加其稳定性。出现了两种主要的假说来解释这种行为：1）螺旋内立体电子效应，以及2）H分子与羟基脯氨酸侧链结合的作用。但是，在凝结阶段研究中，水的影响无法完全消除。因此，我们结合了串联离子迁移率和质谱技术来评估气相中CMP组件的结构和稳定性。这些结果表明在没有溶剂的情况下三螺旋模型的结构和稳定性得到了保留，这支持了立体电子效应的重要作用。此外，有证据表明可以在气相中研究化学计量比可控的小型三重螺旋组件，这为了解胶原纤维生长的第一步开辟了新的前景。