4.7 Article

Differential Self-Assembly Behaviors of Cyclic and Linear Peptides

Journal

BIOMACROMOLECULES
Volume 13, Issue 7, Pages 1991-1995

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/bm3005947

Keywords

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Funding

  1. National Research Foundation (NRF) of Korea [2011-0019125]
  2. Basic Science Research Program [2011-0003540, 2011-0003065, 2012R1A1A2006453]
  3. Translational Research Center for Protein Function Control, Yonsei University [2012-0000888]
  4. Seoul RBD program [ST110029M0212351]

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Here we ask the fundamental questions about the effect of peptide topology on self-assembly. The study revealed that the self-assembling behaviors of cyclic and linear peptides are significantly different in several respects, in addition to sharing several similarities. Their clear differences included the morphological dissimilarities of the self-assembled nanostructures and their thermal stability. The similarities include their analogous critical aggregation concentration values and cytotoxicity profiles, which are in fact closely related. We believe that understanding topology-dependent self-assembly behavior of peptides is important for developing tailor-made self-assembled peptide nanostructures.

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