Cyclization of a cytolytic amphipathic alpha-helical peptide and its diastereomer: effect on structure, interaction with model membranes, and biological function.

@article{Oren2000CyclizationOA,
  title={Cyclization of a cytolytic amphipathic alpha-helical peptide and its diastereomer: effect on structure, interaction with model membranes, and biological function.},
  author={Ziv Oren and Yechiel Shai},
  journal={Biochemistry},
  year={2000},
  volume={39 20},
  pages={6103-14}
}
The amphipathic alpha-helical structure is considered to be a prerequisite for the lytic activity of a large group of cytolytic peptides. However, despite numerous studies on the contribution of various parameters to their structure and activity, the importance of linearity has not been examined. In the present study we functionally and structurally characterized a linear amphipathic alpha-helical peptide (wt peptide), its diastereomer, and cyclic analogues of both. Using analogues with the… CONTINUE READING

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