Maher Malachy Kevin, White Jacinta F, Glattauer Veronica, Yue Zhilian, Hughes Timothy C, Ramshaw John A M, Wallace Gordon G
Intelligent Polymer Research Institute, ARC Centre of Excellence for Electromaterials Science, AIIM Facility, Innovation Campus, University of Wollongong, Wollongong, NSW 2519, Australia.
CSIRO Manufacturing, Clayton, Melbourne, VIC 3168, Australia.
Polymers (Basel). 2022 Apr 27;14(9):1775. doi: 10.3390/polym14091775.
As the most abundant protein in the extracellular matrix, collagen has become widely studied in the fields of tissue engineering and regenerative medicine. Of the various collagen types, collagen type I is the most commonly utilised in laboratory studies. In tissues, collagen type I forms into fibrils that provide an extended fibrillar network. In tissue engineering and regenerative medicine, little emphasis has been placed on the nature of the network that is formed. Various factors could affect the network structure, including the method used to extract collagen from native tissue, since this may remove the telopeptides, and the nature and extent of any chemical modifications and crosslinking moieties. The structure of any fibril network affects cellular proliferation and differentiation, as well as the overall modulus of hydrogels. In this study, the network-forming properties of two distinct forms of collagen (telo- and atelo-collagen) and their methacrylated derivatives were compared. The presence of the telopeptides facilitated fibril formation in the unmodified samples, but this benefit was substantially reduced by subsequent methacrylation, leading to a loss in the native self-assembly potential. Furthermore, the impact of the methacrylation of the collagen, which enables rapid crosslinking and makes it suitable for use in 3D printing, was investigated. The crosslinking of the methacrylated samples (both telo- and atelo-) was seen to improve the fibril-like network compared to the non-crosslinked samples. This contrasted with the samples of methacrylated gelatin, which showed little, if any, fibrillar or ordered network structure, regardless of whether they were crosslinked.
作为细胞外基质中含量最丰富的蛋白质，胶原蛋白在组织工程和再生医学领域受到了广泛研究。在各种胶原蛋白类型中，I型胶原蛋白是实验室研究中最常用的。在组织中，I型胶原蛋白形成纤维，提供一个扩展的纤维网络。在组织工程和再生医学中，人们很少关注所形成网络的性质。各种因素可能会影响网络结构，包括从天然组织中提取胶原蛋白的方法，因为这可能会去除端肽，以及任何化学修饰和交联部分的性质和程度。任何纤维网络的结构都会影响细胞增殖和分化，以及水凝胶的整体模量。在本研究中，比较了两种不同形式的胶原蛋白（端肽胶原蛋白和非端肽胶原蛋白）及其甲基丙烯酸化衍生物的网络形成特性。端肽的存在促进了未修饰样品中的纤维形成，但随后的甲基丙烯酸化大大降低了这种益处，导致天然自组装潜力丧失。此外，还研究了胶原蛋白甲基丙烯酸化的影响，它能够实现快速交联，使其适用于3D打印。与未交联的样品相比，甲基丙烯酸化样品（端肽胶原蛋白和非端肽胶原蛋白）的交联被认为改善了纤维状网络。这与甲基丙烯酸化明胶样品形成对比，无论是否交联，甲基丙烯酸化明胶样品几乎没有显示出纤维状或有序的网络结构。
