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

  1. Author:
    Lee, Y.
    Chen, Y. H.
    Tarasova, N. I.
    Gaponenko, V.

  2. Author Address

    [Lee, Youngshim; Gaponenko, Vadim] Univ Illinois, Dept Biochem & Mol Genet, Chicago, IL 60607 USA. [Chen, Yuhong; Tarasova, Nadya I.] NCI, Canc & Inflammat Program, Frederick, MD 21702 USA.;Gaponenko, V (reprint author), Univ Illinois, Dept Biochem & Mol Genet, 900 S Ashland Ave, Chicago, IL 60607 USA;vadimg@uic.edu
    1. Year: 2011
    2. Date: Dec
  2. Journal: Nanotechnology
    1. 22
    2. 50
  4. Type of Article: Article
  5. Article Number: 505101
  6. ISSN: 0957-4484
  1. 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.

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External Sources

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  2. DOI: 10.1088/0957-4484/22/50/505101
  3. View record in Web of Science®
  4. WOS: 000298154200001

Library Notes

  1. Fiscal Year: FY2011-2012
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