Medini Karima, Mansel Bradley W, Williams Martin A K, Brimble Margaret A, Williams David E, Gerrard Juliet A
School of Chemical Sciences, The University of Auckland, 23 Symonds St., Auckland 1010, New Zealand; School of Biological Sciences, The University of Auckland, 3A Symonds St., Auckland 1010, New Zealand; MacDiarmid Institute for Advanced Materials and Nanotechnology, Victoria University, Wellington 6140, New Zealand.
Institute of Fundamental Sciences, Massey University, Palmerston North 4442, New Zealand.
Acta Biomater. 2016 Oct 1;43:30-37. doi: 10.1016/j.actbio.2016.07.021. Epub 2016 Jul 14.
The self-assembling peptide IKHLSVN, inspired by inspection of a protein-protein interface, has previously been reported as one of a new class of bio-inspired peptides. Here the peptide, dubbed littleSven, and modifications designed to probe the resilience of the sequence to self-assembly, is characterised. Although the parent peptide did not form a hydrogel, small modifications to the sequence (one side chain or an N-terminus modification) led to hydrogels with properties (eg. gelation time and rheology) that could be tuned by these small alterations. The results suggest that peptides derived from protein-protein interfaces are resilient to changes in sequence and can be harnessed to form hydrogels with controlled properties.
Natural occurring self-assembly peptides are attractive building blocks for engineered bionanomaterials due to their biocompatibility and biodegradability. The bio-inspired self-assembly peptide, IKHLSVN, was used as a template to design peptides that readily formed hydrogels. The peptide sequence was specifically tuned to create a bionanomaterial with different properties that could be exploited downstream for a broad range of applications: nanowires, drug release, vaccine adjuvant, tissue engineering. We describe how small modifications to the parent peptide alter the amyloid-like characteristics and gel strength for each peptide.
通过对蛋白质-蛋白质界面的研究获得灵感的自组装肽IKHLSVN，此前已被报道为一类新型生物启发肽之一。在此，对该被称为小斯文（littleSven）的肽以及为探究序列对自组装的适应性而设计的修饰进行了表征。尽管亲本肽未形成水凝胶，但对序列进行小的修饰（一个侧链或N端修饰）会导致形成具有可通过这些小改变进行调节的特性（如凝胶化时间和流变学）的水凝胶。结果表明，源自蛋白质-蛋白质界面的肽对序列变化具有适应性，可用于形成具有可控特性的水凝胶。
天然存在的自组装肽由于其生物相容性和生物可降解性，是工程化生物纳米材料的有吸引力的构建块。以生物启发的自组装肽IKHLSVN为模板设计了易于形成水凝胶的肽。对肽序列进行了特定调整，以创建一种具有不同特性的生物纳米材料，可在下游用于广泛的应用：纳米线、药物释放、疫苗佐剂、组织工程。我们描述了对亲本肽的小修饰如何改变每种肽的淀粉样特征和凝胶强度。
