title: The structure of monomeric components of self-assembling CXCR4 antagonists determines the architecture of resulting nanostructures.
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.
authors: Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL 60607, USA.
authors: Youngshim
authors: Y
authors: Lee
authors: Yuhong
authors: Y
authors: Chen
authors: Nadya I
authors: NI
authors: Tarasova
authors: Vadim
authors: V
authors: Gaponenko
mesh_terms: D000595:Amino Acid Sequence; D004337:Drug Carriers / Q000138:chemical synthesis / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D054118:Nanospheres / Q000737:chemistry; D049329:Nanostructures / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011721:Pyrenes; D019718:Receptors, CXCR4 / Q000037:antagonists & inhibitors*; D016415:Sequence Alignment; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship
chemical_list: D004337:Drug Carriers; D010455:Peptides; D011721:Pyrenes; D019718:Receptors, CXCR4; C030984:pyrene