Journal
CHEMBIOCHEM
Volume 5, Issue 9, Pages 1245-1255Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.200400025
Keywords
carbohydrate binding; chitin; hevein; molecular dynamics; NMR spectroscopy
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HEV32, a 32-residue, truncated hevein locking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments-in the forms of N,N',N-triacetylchitotriose ((GlcNAc)(3)) (millimolar) and N,N',N,N',N,N'-hexaacetylchitohexaose ((GlcNAc)(6)) (micromolar)-as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein.
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