Nanostructures Formed by Custom-Made Peptides Based on Amyloid Peptide Sequences and Their Inhibition by 2-Hydroxynaphthoquinone
Nanostructures Formed by Custom-Made Peptides Based on Amyloid Peptide Sequences and Their Inhibition by 2-Hydroxynaphthoquinone
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DOI：
10.3389/fchem.2020.00684
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发表时间：
2020-08-06
影响因子：
5.5
通讯作者：
Sreerama, Lakshmaiah
中科院分区：
文献类型：
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作者：
Mannem, Radhika;Yousuf, Mohammed;Sreerama, Lakshmaiah
对淀粉样纤维形成的广泛研究表明，A β肽内的某些核心序列在其形成中起重要作用。这是不可能的跟踪这些evenably vivo。具有这种核心序列的许多蛋白质和肽形成淀粉样蛋白原纤维，并且这种A β折叠模拟物已经成为研究淀粉样蛋白原纤维形成和开发治疗策略的极好工具。通过SEM和ThT结合试验测试基于PDB搜索获得的淀粉样肽序列的一组肽的聚集，其中甘氨酸残基被丙氨酸和异亮氨酸取代。不同肽序列的SEM显示形态上不同的结构，如纳米棒，结晶针和纳米纤维。将肽与HNQ（醌）共孵育以研究其对聚集和/或原纤化过程的影响。总之，这组肽似乎是A β片层模拟物，并且在理解由不同肽序列产生的淀粉样蛋白原纤维的不同形态以及抑制或退火它们的有效策略方面非常有用。
Extensive research on amyloid fibril formations shows that certain core sequences within A beta peptide play an important role in their formation. It is impossible to track these eventsin vivo. Many proteins and peptides with such core sequences form amyloid fibrils and such A beta sheet mimics have become excellent tools to study amyloid fibril formation and develop therapeutic strategies. A group of peptides based on amyloid peptide sequences obtained from PDB searches, where glycine residues are substituted with alanine and isoleucine, are tested for aggregation by SEM and ThT binding assay. SEM of different peptide sequences showed morphologically different structures such as nanorods, crystalline needles and nanofibrils. The peptides were co-incubated with HNQ (a quinone) to study its effect on the process of aggregation and/or fibrillation. In conclusion, this group of peptides seem to be A beta sheet mimics and can be very useful in understanding the different morphologies of amyloid fibrils arising from different peptide sequences and the effective strategies to inhibit or anneal them.