Artificial Peptide-Nanospheres Self-Assembled from Three-Way Junctions of β-Sheet-Forming Peptides
Rational design of self-assembly of proteins, which plays pivotal roles in biology, is an important subject for biotechnology and also bottom-up nanotechnology. This paper has proposed a novel strategy for construction of artificial peptide-nanospheres by self-assembly. Mimicking formation of spheri...
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| Published in | Journal of the American Chemical Society Vol. 127; no. 29; pp. 10148 - 10149 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
WASHINGTON
American Chemical Society
27.07.2005
Amer Chemical Soc |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0002-7863 1520-5126 |
| DOI | 10.1021/ja052644i |
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| Abstract | Rational design of self-assembly of proteins, which plays pivotal roles in biology, is an important subject for biotechnology and also bottom-up nanotechnology. This paper has proposed a novel strategy for construction of artificial peptide-nanospheres by self-assembly. Mimicking formation of spherical viruses and clathrin, we designed a novel C 3-symmetric peptide conjugate bearing three β-sheet-forming peptides. These peptide conjugates formed antiparallel β-structures and self-assembled into nanospheres with the size of about 20 nm in the acidic solution. |
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| AbstractList | Rational design of self-assembly of proteins, which plays pivotal roles in biology, is an important subject for biotechnology and also bottom-up nanotechnology. This paper has proposed a novel strategy for construction of artificial peptide-nanospheres by self-assembly. Mimicking formation of spherical viruses and clathrin, we designed a novel C sub(3)-symmetric peptide conjugate bearing three beta -sheet-forming peptides. These peptide conjugates formed antiparallel beta -structures and self-assembled into nanospheres with the size of about 20 nm in the acidic solution. Rational design of self-assembly of proteins, which plays pivotal roles in biology, is an important subject for biotechnology and also bottom-up nanotechnology. This paper has proposed a novel strategy for construction of artificial peptide-nanospheres by self-assembly. Mimicking formation of spherical viruses and clathrin, we designed a novel C 3-symmetric peptide conjugate bearing three β-sheet-forming peptides. These peptide conjugates formed antiparallel β-structures and self-assembled into nanospheres with the size of about 20 nm in the acidic solution. Rational design of self-assembly of proteins, which plays pivotal roles in biology, is an important subject for biotechnology and also bottom-up nanotechnology. This paper has proposed a novel strategy for construction of artificial peptide-nanospheres by self-assembly. Mimicking formation of spherical viruses and clathrin, we designed a novel C3-symmetric peptide conjugate bearing three beta-sheet-forming peptides. These peptide conjugates formed antiparallel beta-structures and self-assembled into nanospheres with the size of about 20 nm in the acidic solution. Rational design of self-assembly of proteins, which plays pivotal roles in biology, is an important subject for biotechnology and also bottom-up nanotechnology. This paper has proposed a novel strategy for construction of artificial peptide-nanospheres by self-assembly. Mimicking formation of spherical viruses and clathrin, we designed a novel C3-symmetric peptide conjugate bearing three beta-sheet-forming peptides. These peptide conjugates formed antiparallel beta-structures and self-assembled into nanospheres with the size of about 20 nm in the acidic solution.Rational design of self-assembly of proteins, which plays pivotal roles in biology, is an important subject for biotechnology and also bottom-up nanotechnology. This paper has proposed a novel strategy for construction of artificial peptide-nanospheres by self-assembly. Mimicking formation of spherical viruses and clathrin, we designed a novel C3-symmetric peptide conjugate bearing three beta-sheet-forming peptides. These peptide conjugates formed antiparallel beta-structures and self-assembled into nanospheres with the size of about 20 nm in the acidic solution. |
| Author | Matsuura, Kazunori Kimizuka, Nobuo Murasato, Kazuya |
| Author_xml | – sequence: 1 givenname: Kazunori surname: Matsuura fullname: Matsuura, Kazunori – sequence: 2 givenname: Kazuya surname: Murasato fullname: Murasato, Kazuya – sequence: 3 givenname: Nobuo surname: Kimizuka fullname: Kimizuka, Nobuo |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16988867$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/16028908$$D View this record in MEDLINE/PubMed |
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| Keywords | NANOPARTICLES DESIGN CAGE FIBRILS AMPHIPHILES CLATHRIN Atomic force microscopy Supramolecular structure Biopolymer Molecular association Molecular interaction Molecular aggregation Nanosphere Polyaminoacid Amphiphilic polymer |
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| Snippet | Rational design of self-assembly of proteins, which plays pivotal roles in biology, is an important subject for biotechnology and also bottom-up... |
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| SubjectTerms | Biological and medical sciences Chemistry Chemistry, Multidisciplinary Circular Dichroism Fundamental and applied biological sciences. Psychology Interactions. Associations Intermolecular phenomena Microscopy, Atomic Force Models, Molecular Molecular biophysics Nanotubes - chemistry Oligopeptides - chemistry Physical Sciences Protein Structure, Secondary Science & Technology |
| Title | Artificial Peptide-Nanospheres Self-Assembled from Three-Way Junctions of β-Sheet-Forming Peptides |
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