Supramolecular helical self-assembly of small peptides

被引:9
|
作者
Giri, Rajat Subhra [1 ]
Mandal, Bhubaneswar [1 ]
机构
[1] Indian Inst Technol Guwahati, Lab Peptide & Amyloid Res, Dept Chem, Gauhati 781039, Assam, India
关键词
1ST CRYSTALLOGRAPHIC SIGNATURE; SIDE-CHAIN INTERACTIONS; BETA-PEPTIDE; BUILDING-BLOCKS; NUCLEIC-ACIDS; IN-VITRO; COLLAGEN; SHEET; AIB; TETRAPEPTIDES;
D O I
10.1039/d1ce01349a
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The self-assembly of peptides forming various micro to nanostructures has several applications in nanobiotechnology. beta-Sheet based peptides are well known as they are abundant in nature, e.g., silk and amyloid fibrils. Therefore, the self-assembly of small beta-sheet peptides and their potent applications are well explored to date. On the other hand, various helical secondary structures are also abundant in nature. Like beta-sheet peptides, small peptide-based helical assemblies are not explored enough, but they also attract attention for fabricating various artificial nanomaterials in recent times. This highlight focuses on single-crystal X-ray diffraction (SC-XRD) based analysis of the supramolecular arrangement, conformation, and higher-order assembly of small helical peptides. We outline the role of building blocks and their structural beauty to adopt helical assembly, including single-, double- and triple-stranded helices. We also describe their micro or nano-level structures obtained from the solution and their potent applications as drug delivery vehicles, as porous materials for N-2 adsorption, and for nanomaterial fabrication.
引用
收藏
页码:10 / 32
页数:23
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