Melittin as Model System for Probing Interactions between Proteins and Cyclodextrins

Mazdak Khajehpour, Thomas Troxler, Vikas Nanda, Jane M. Vanderkooi

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

Cylcodextrin sugars are cyclic sugars that have a hydrophilic exterior and a hydrophobic center. This enables cyclodextrins to solubilize hydrophobic molecules in aqueous media. Cyclodextrins may inhibit aggregation by intercalating surface aromatic residues and competing with interprotein aromatic clusters (π-π interactions). In order to investigate this concept, the interaction of hydroxypropyl-β-cyclodextrin (HPBCD) with melittin is studied with steady-state and time-resolved fluorescence, fluorescence polarization, circular dichroism, and IR spectroscopy. HPBCD inhibits the aggregation of melittin. This inhibition and the spectroscopic results are consistent with the lone aromatic tryptophan of the peptide being intercalated within HPBCD.

Original languageEnglish (US)
Pages (from-to)275-287
Number of pages13
JournalProteins: Structure, Function and Genetics
Volume55
Issue number2
DOIs
StatePublished - May 1 2004

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Keywords

  • Cyclodextrin
  • Fluorescence
  • Melittin
  • Peptide aggregation

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