Research Article

Melittin as model system for probing interactions between proteins and cyclodextrins

  1. Mazdak Khajehpour1,*,
  2. Thomas Troxler2,
  3. Vikas Nanda1,
  4. Jane M. Vanderkooi1

Article first published online: 27 FEB 2004

DOI: 10.1002/prot.20036

Issue

Proteins: Structure, Function, and Bioinformatics

Proteins: Structure, Function, and Bioinformatics

Volume 55, Issue 2, pages 275–287, 1 May 2004

Additional Information

How to Cite

Khajehpour, M., Troxler, T., Nanda, V. and Vanderkooi, J. M. (2004), Melittin as model system for probing interactions between proteins and cyclodextrins. Proteins: Structure, Function, and Bioinformatics, 55: 275–287. doi: 10.1002/prot.20036

Author Information

  1. 1

    Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104

  2. 2

    Regional Laser and Biotechnology Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104

*Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104

Publication History

  1. Issue published online: 18 MAR 2004
  2. Article first published online: 27 FEB 2004
  3. Manuscript Accepted: 27 AUG 2003
  4. Manuscript Revised: 29 JUL 2003
  5. Manuscript Received: 15 MAY 2003

Funded by

  • NIH. Grant Number: PO1 48130

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Keywords:

  • cyclodextrin;
  • melittin;
  • peptide aggregation;
  • fluorescence

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. Proteins 2004. © 2004 Wiley-Liss, Inc.

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