NMR solution structure of the angiostatic peptide anginex

Monica M. Arroyo, Kevin H Mayo

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Anginex, a designed peptide 33mer, is known to function both as an antiangiogenic and bactericidal agent. Solving the NMR solution structure of the peptide is key to understand better its structure-activity relationships and to design more bioactive peptides and peptide mimetics. However, structure elucidation of anginex has been elusive due to subunit exchange-induced resonance broadening. Here, we found that performing NMR structural studies in a micellar environment abolishes exchange broadening and allows the structure of anginex to be determined. Anginex folds in an amphipathic, three-stranded antiparallel β-sheet conformation with functionally key hydrophobic residues lying on one face of the β-sheet and positively charged, mostly lysine residues, lying on the opposite face. Structural comparison is made with a homologous, yet relatively inactive peptide, βpep-28. These results contribute to the design of peptidomimetics of anginex for therapeutic use against angiogenically-related diseases like cancer, as well as infectious diseases.

Original languageEnglish (US)
Pages (from-to)645-651
Number of pages7
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Issue number5
StatePublished - May 2007

Bibliographical note

Funding Information:
This work was supported by support from the National Institutes of Health (NIH CA-96090 and AI-057153). NMR instrumentation was provided with funds from the NSF (BIR-961477) and the University of Minnesota Medical School. Peptides were synthesized at the Microchemical Facility, University of Minnesota.


  • Anti-angiogenic
  • Anti-bacterial
  • Conformation
  • Drug design


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