Golser Adrian V, Röber Matthias, Börner Hans G, Scheibel Thomas
Lehrstuhl Biomaterialien, Fakultät für Ingenieurwissenschaften Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany.
Laboratory for Organic Synthesis of Functional Systems, Department of Chemistry Humboldt-Universität zu Berlin, Brook-Taylor-Strasse 2, 12489 Berlin, Germany.
ACS Biomater Sci Eng. 2018 Jun 11;4(6):2106-2114. doi: 10.1021/acsbiomaterials.7b00583. Epub 2018 May 9.
Collagen, processed into several morphologies and originating from various sources, has long since been used as a biocompatible material that can assist wound healing and tissue regeneration. With the advent of biotechnology and solid-phase peptide synthesis, new possibilities arise to create rationally designed biomaterials based on collagen sequences incorporating new functionalities while maintaining the beneficial properties of natural collagen. In this study a new class of synthetic collagen materials is presented, defined by its simplistic core structure and its therefore predictable behavior. These so-called eCols (engineered collagens) consist of a varying number of Gly-Pro-Pro repeats, a redox-switchable aminoterminal nucleation site and an optional carboxyterminal cell adhesion motif. We show which of these proteins are able to self-assemble into triple helices and cross-linked gelatinous networks and provide insights into their cytocompatibility in vitro.
胶原蛋白经过加工形成多种形态，来源各异，长期以来一直被用作生物相容性材料，可辅助伤口愈合和组织再生。随着生物技术和固相肽合成的出现，出现了新的可能性，即基于胶原蛋白序列设计合理的生物材料，在保持天然胶原蛋白有益特性的同时融入新功能。在本研究中，提出了一类新型合成胶原蛋白材料，其定义为具有简单的核心结构以及可预测的行为。这些所谓的eCols（工程胶原蛋白）由不同数量的甘氨酸-脯氨酸-脯氨酸重复序列、一个氧化还原可切换的氨基末端成核位点和一个可选的羧基末端细胞粘附基序组成。我们展示了这些蛋白质中哪些能够自组装成三螺旋和交联凝胶网络，并深入了解它们在体外的细胞相容性。
