Journal
BIOMACROMOLECULES
Volume 13, Issue 7, Pages 1991-1995Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bm3005947
Keywords
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Funding
- National Research Foundation (NRF) of Korea [2011-0019125]
- Basic Science Research Program [2011-0003540, 2011-0003065, 2012R1A1A2006453]
- Translational Research Center for Protein Function Control, Yonsei University [2012-0000888]
- 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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