Back to Search
Start Over
Self-assembly of Functional Nanostructures by Short Helical Peptide Building Blocks
- Source :
- Protein & Peptide Letters, Protein and Peptide Letters
-
Abstract
- The self-assembly of short peptide building blocks into well-ordered nanostructures is a key direction in bionanotechnology. The formation of β -sheet organizations by short peptides is well explored, leading to the development of a wide range of functional assemblies. Likewise, many natural proteinaceous materials, such as silk and amyloid fibrils, are based on β-sheet structures. In contrast, collagen, the most abundant protein in mammals, is based on helical arrangement. Similar to β-sheet structures, short helical peptides have been recently discovered to possess a diverse set of functionalities with the potential to fabricate artificial self-assembling materials. Here, we outline the functional roles of self-assembled nanostructures formed by short helical peptides and their potential as artificial materials. We focus on the association between self-assembled mesoscale structures and their material function and demonstrate the way by which this class of building blocks bears the potential for diverse applications, such as the future fabrication of smart devices.
- Subjects :
- Amyloid
Materials science
Nanostructure
nanostructure
Protein Conformation
Surface Properties
β-sheet structure
Nanotechnology
Peptide
02 engineering and technology
010402 general chemistry
01 natural sciences
Biochemistry
Article
Drug Delivery Systems
Structural Biology
Nanobiotechnology
Helical peptide
chemistry.chemical_classification
Artificial materials
nanotechnology
Self-assembly
helical conformation
General Medicine
021001 nanoscience & nanotechnology
Amyloid fibril
Nanostructures
0104 chemical sciences
SILK
chemistry
Protein Conformation, beta-Strand
Collagen
short peptide
Protein Multimerization
Peptides
0210 nano-technology
Subjects
Details
- Language :
- English
- ISSN :
- 09298665
- Volume :
- 26
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Protein & Peptide Letters
- Accession number :
- edsair.doi.dedup.....528746d1c566bcc4ba7d51fb4b0ef1aa
- Full Text :
- https://doi.org/10.2174/0929866525666180917163142