Department of Organic Chemistry, Faculty of Chemistry, University of Gdansk, 80-308 Gdansk, Poland.
Institute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, Poland.
Int J Mol Sci. 2022 May 22;23(10):5800. doi: 10.3390/ijms23105800.
Amyloid fibrils have been known for many years. Unfortunately, their fame stems from negative aspects related to amyloid diseases. Nevertheless, due to their properties, they can be used as interesting nanomaterials. Apart from their remarkable stability, amyloid fibrils may be regarded as a kind of a storage medium and as a source of active peptides. In many cases, their structure may guarantee a controlled and slow release of peptides in their active form; therefore, they can be used as a potential nanomaterial in drug delivery systems. In addition, amyloid fibrils display controllable stiffness, flexibility, and satisfactory mechanical strength. In addition, they can be modified and functionalized very easily. Understanding the structure and genesis of amyloid assemblies derived from a broad range of amyloidogenic proteins could help to better understand and use this unique material. One of the factors responsible for amyloid aggregation is the steric zipper. Here, we report the discovery of steric zipper-forming peptides in the sequence of the amyloidogenic protein, human cystatin C (HCC). The ability of short peptides derived from this fragment of HCC to form fibrillar structures with defined self-association characteristics and the factors influencing this aggregation are also presented in this paper.
淀粉样纤维多年来广为人知。不幸的是，它们的名气源于与淀粉样变性疾病相关的负面方面。尽管如此，由于其特性，它们可以被用作有趣的纳米材料。除了显著的稳定性外，淀粉样纤维还可以被视为一种储存介质和活性肽的来源。在许多情况下，其结构可以保证肽以活性形式的受控和缓慢释放；因此，它们可以用作药物传递系统中的潜在纳米材料。此外，淀粉样纤维表现出可控的刚性、柔韧性和令人满意的机械强度。此外，它们可以非常容易地进行修饰和功能化。了解源自广泛淀粉样蛋白的淀粉样组装体的结构和成因，有助于更好地理解和利用这种独特的材料。导致淀粉样聚集的因素之一是空间拉链。在这里，我们报告了在淀粉样蛋白，人半胱氨酸蛋白酶抑制剂 C（HCC）的序列中发现了形成空间拉链的肽。本文还介绍了源自 HCC 片段的短肽形成具有确定自组装特征的纤维状结构的能力以及影响这种聚集的因素。
