The structure of monomeric components of self-assembling CXCR4 antagonists determinesthe architecture of resulting nanostructures

Abstract

Self-assembling peptides play increasingly important roles in the development of novelmaterials and drug delivery vehicles. Understanding mechanisms governing the assembly ofnanoarchitectures is essential for the generation of peptide-based nanodevices. We find thata cone-shaped derivative of the second transmembrane domain of CXCR4 receptor, x4-2-6self-assembles into nanospheres, while a related cylindrical peptide, x4-2-9 formsfibrils. Stronger intermolecular interactions in nanospheres than in fibrils result inslow rates of particle disassembly and protection against proteolytic degradation.