Differential self-assembly behaviors of cyclic and linear peptides.
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.
Translational Research Center for Protein Function Control and Department of Materials Science & Engineering, Yonsei University, Seoul, Korea.
Sung-ju
SJ
Choi
Woo-jin
WJ
Jeong
Seong-Kyun
SK
Kang
Myongsoo
M
Lee
Eunhye
E
Kim
Du Yeol
du Y
Ryu
Yong-beom
YB
Lim
D000595:Amino Acid Sequence; D002470:Cell Survival / Q000187:drug effects; D006367:HeLa Cells; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry / Q000648:ultrastructure; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D013501:Surface-Active Agents / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology
D009842:Oligopeptides; D010456:Peptides, Cyclic; D013501:Surface-Active Agents