School of Materials, ‡Manchester Institute of Biotechnology, and ∥School of Chemical Engineering and Analytical Sciences, The University of Manchester , Oxford Road, Manchester, M13 9PL, United Kingdom.
Biomacromolecules. 2017 Mar 13;18(3):826-834. doi: 10.1021/acs.biomac.6b01693. Epub 2017 Feb 3.
Self-assembling peptide-based hydrogels have encountered increasing interest in the recent years as scaffolds for 3D cell culture or for controlled drug delivery. One of the main challenges is the fine control of the mechanical properties of these materials. The bulk properties of hydrogels not only depend on the intrinsic properties of the fibers but also on the network topology formed. In this work we show how fiber-fiber interactions can be manipulated by design to control the final hydrogel network topology and therefore control the final properties of the material. This was achieved by exploiting the design features of β-sheet forming peptides based on hydrophobic and hydrophilic residue alternation and exploiting the ability of the arginine's guanidine side group to interact with itself and with other amino acid side groups. By designing octa-peptides based on phenylalanine, glutamic acid, lysine, and arginine, we have investigated how fiber association and bundling affect the dynamic shear modulus of hydrogels and how it can be controlled by design. This work opens the possibility to fine-tune by design the bulk properties of peptide hydrogels.
近年来，基于自组装肽的水凝胶作为 3D 细胞培养支架或控制药物释放的载体，受到了越来越多的关注。其中一个主要挑战是精细控制这些材料的机械性能。水凝胶的整体性质不仅取决于纤维的固有性质，还取决于形成的网络拓扑结构。在这项工作中，我们展示了如何通过设计来操纵纤维-纤维相互作用，从而控制最终水凝胶网络拓扑结构，并最终控制材料的性能。这是通过利用基于疏水性和亲水性残基交替的 β-折叠形成肽的设计特点以及精氨酸的胍侧基与自身和其他氨基酸侧基相互作用的能力来实现的。通过设计基于苯丙氨酸、谷氨酸、赖氨酸和精氨酸的八肽，我们研究了纤维缔合和束集如何影响水凝胶的动态剪切模量，以及如何通过设计进行控制。这项工作为通过设计精细调整肽水凝胶的整体性质提供了可能性。
