Controlling Self-Assembling Peptide Hydrogel Properties through Network Topology
Controlling Self-Assembling Peptide Hydrogel Properties through Network Topology
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DOI：
10.1021/acs.biomac.6b01693
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发表时间：
2017-03-01
影响因子：
6.2
通讯作者：
Saiani, Alberto
中科院分区：
文献类型：
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作者：
Gao, Jie;Tang, Claire;Saiani, Alberto
近年来，自组装肽基水凝胶作为 3D 细胞培养或受控药物输送的支架引起了越来越多的兴趣。主要挑战之一是这些材料的机械性能的精细控制。水凝胶的整体特性不仅取决于纤维的固有特性，还取决于形成的网络拓扑。在这项工作中，我们展示了如何通过设计来操纵纤维相互作用，以控制最终的水凝胶网络拓扑，从而控制材料的最终性能。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征以及利用精氨酸的胍侧基与其自身以及与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成束如何影响水凝胶的动态剪切模量以及如何通过设计控制它。这项工作为通过设计微调肽水凝胶的整体特性提供了可能性。
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 beta-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.