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Controlled bioactive nanostructures from self-assembly of peptide building blocks.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Lim, Yong-Beom Lee, Eunji Lee, Myongsoo |
| Copyright Year | 2007 |
| Abstract | Molecular self-assembly has become one of the most intensive areas of research during recent years. This is, in part, due to its vast potential for use in many industrial and biotechnological applications. For biotechnological applications of self-assembled supramolecular nanostructures, the exterior of the nanostructures should be coated with bioactive molecules to construct functional materials. Among many bioactive molecules that could be used, coating of the nanostructures with peptides provides unique opportunities to explore the myriads of biological events that peptides mediate. The discovery of a general strategy to assemble functional peptides into stable nanostructures with desired size and shape should be one of the most important issues in developing peptide-based self-assembly systems. It can be speculated that the larger and more highly charged peptides demand stronger hydrophobic interactions for stable selfassembly. Herein, we report on versatile strategies for the selfassembly of any type of large and highly charged peptides and for the control of the sizes and morphologies of peptidecoated nanostructures. To address this, we synthesized a novel class of several supramolecular building blocks which consist of a functional peptide and a hydrophobic lipid dendrimer. As the functional peptide, we selected Tat cell-penetrating peptide (Tat CPP), a well-known CPP from human immunodeficiency virus type-1 (HIV-1). The 13-mer Tat CPP (Tat48– 60) is a highly charged peptide with 8 positive residues (2 lysines and 6 arginines). One of the advantages of Tat CPP is that it can be translocated efficiently in the cell nucleus, as well as in the cell cytoplasm. Many efforts have been made to utilize Tat CPP for delivering bioactive molecules, either by direct conjugation of the bioactive molecules with Tat CPP or by dendrimer and nanoparticle display of Tat CPP. Another important biological activity of Tat CPP is that the CPP domain of Tat protein binds specifically to the HIV-1 trans-acting response element (TAR) RNA hairpin. As binding of Tat protein to viral mRNA at the TAR is essential for viral transcription and replication, the development of inhibitors of this interaction has been the subject of anti-HIV drug discovery. In the self-assembly of conventional amphiphilic block copolymers, the length and composition of each block affects the stability (aggregation strength), size, and shape of the nanostructures. To systematically study the effect of the relative composition of the hydrophobic blocks in peptide block molecules on the stability and supramolecular morphology, we dendritically increased the number of lipid molecules (stearic acid, C18) attached to the N terminus of Tat CPP from one to four, thereby yielding TLD-m (monobranch), TLD-d (dibranch), and TLD-t (tetrabranch; Figure 1). The TLDs consist of three blocks, a biofunctional Tat CPP, a flexible linker (e-aminohexanoic acid), and a lipid chain. All of the TLDs were soluble in water. |
| File Format | PDF HTM / HTML |
| DOI | 10.1002/anie.200702732 |
| PubMed reference number | 17948317 |
| Journal | Medline |
| Volume Number | 46 |
| Issue Number | 47 |
| Alternate Webpage(s) | https://web.yonsei.ac.kr/bionano/Publication/19.%20(Angew%20chem,07)%20Controlled%20bioactive%20nanostructures%20from%20self-assembly%20of%20peptide%20building%20blocks.pdf |
| Alternate Webpage(s) | https://doi.org/10.1002/anie.200702732 |
| Journal | Angewandte Chemie |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
