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Melittin as model system for probing interactions between proteins and cyclodextrins
Author(s) -
Khajehpour Mazdak,
Troxler Thomas,
Nanda Vikas,
Vanderkooi Jane M.
Publication year - 2004
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20036
Subject(s) - melittin , chemistry , circular dichroism , tryptophan , cyclodextrin , fluorescence , hydrophobic effect , fluorescence spectroscopy , molecule , fluorescence anisotropy , aqueous solution , peptide , crystallography , biophysics , organic chemistry , stereochemistry , membrane , amino acid , biochemistry , physics , quantum mechanics , biology
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.