Structured Cyclic Peptides That Bind the EH Domain of EHD1

Details

• Alternative Title:
  Biochemistry
• Personal Author:
  Kamens, Alissa J. ; Eisert, Robyn J. ; Corlin, Tiffany ; Baleja, James D. ; Kritzer, Joshua A.
• Description:
  EHD1 mediates long-loop recycling of many receptors by forming signaling complexes using its EH domain. We report the design and optimization of cyclic peptides as ligands for the EH domain of EHD1. We demonstrate that the improved affinity from cyclization allows fluorescence-based screening applications for EH domain inhibitors. The cyclic peptide is also unusually well-structured in aqueous solution, as demonstrated using nuclear magnetic resonance-based structural models. Because few EH domain inhibitors have been described, these more potent inhibitors will improve our understanding of the roles of EHD1 in the context of cancer invasion and metastasis.
• Subjects:
  • Rapid Report
  • Humans
  • Ligands
  • Models, Molecular
  • Peptides, Cyclic
  • Protein Binding
  • Protein Structure, Tertiary
  • Structure-Activity Relationship
  • Vesicular Transport Proteins
• Source:
  Biochemistry. 2014; 53(29):4758-4760.
• Pubmed ID:
  25014215
• Pubmed Central ID:
  PMC4116148
• Document Type:
  Journal Article
• Funding:
  DP2 OD007303/OD/NIH HHS/United States ; DP2-0D007303/DP/NCCDPHP CDC HHS/United States
• Volume:
  53
• Issue:
  29
• Download URL:
  https://stacks.cdc.gov/view/cdc/32095/cdc_32095_DS1.pdf
• File Type:
  [PDF - 1.26 MB]
• Collection(s):
  CDC Public Access
• Main Document Checksum:
  urn:sha256:f3a689cbe587de76006956039b9de879e55a77500ab95e50649ce88eb99340d3