The structure of monomeric components of self-assembling CXCR4 antagonists determines the architecture of resulting nanostructures
Year: 2011
Type: article
Abstract: Self-assembling peptides play increasingly important roles in the development of novel materials and drug delivery vehicles. Understanding mechanisms governing the assembly of nanoarchitectures is essential for the generation of peptide-based nanodevices. We find that a cone-shaped derivative of the second transmembrane domain of CXCR4 receptor, x4-2-6 self-assembles into nanospheres, while a related cylindrical peptide, x4-2-9 forms fibrils. Stronger intermolecular interactions in nanospheres than in fibrils result in slow rates of particle disassembly and protection against proteolytic degradation.
Source: Nanotechnology
Institutions: University of Illinois Chicago, National Cancer Institute
Language: English
Subfield: Biomaterials
Field: Materials Science
Domain: Physical Sciences
Open Access status: green
Awards: G507424362, G7853962322, G9000173260
OpenAlex ID: W2138669459
