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Media type:
E-Article
Title:
Peptide‐Based Carbohydrate Receptors
Contributor:
Rauschenberg, Melanie;
Bandaru, Sateesh;
Waller, Mark P.;
Ravoo, Bart Jan
imprint:
Wiley, 2014
Published in:Chemistry – A European Journal
Language:
English
DOI:
10.1002/chem.201303777
ISSN:
1521-3765;
0947-6539
Origination:
Footnote:
Description:
<jats:title>Abstract</jats:title><jats:p>A broad spectrum of physiological processes is mediated by highly specific noncovalent interactions of carbohydrates and proteins. In a recent communication we identified several cyclic hexapeptides in a dynamic combinatorial library that interact selectively with carbohydrates with high binding constants in water. Herein, we report a detailed investigation of the noncovalent interaction of two cyclic hexapeptides (Cys‐His‐Cys (which we call HisHis) and Cys‐Tyr‐Cys (which we call TyrTyr)) with a selection of monosaccharides and disaccharides in aqueous solution. The parallel and antiparallel isomers of HisHis or TyrTyr were synthesized separately, and their interaction with monosaccharides and disaccharides in aqueous solution was studied by isothermal titration calorimetry, NMR spectroscopic titrations, and circular dichroism spectroscopy. From these measurements, we identified particularly stable complexes (<jats:italic>K</jats:italic><jats:sub>a</jats:sub>>1000 <jats:sc>M</jats:sc><jats:sup>−1</jats:sup>) of the parallel isomer of HisHis with <jats:italic>N</jats:italic>‐acetylneuraminic acid and with methyl‐α‐<jats:sc>D</jats:sc>‐galactopyranoside as well as of both isomers of TyrTyr with trehalose. To gain further insight into the structure of the peptide–carbohydrate complexes, structure prediction was performed using quantum chemical methods. The calculations confirm the selectivity observed in the experiments and indicate the formation of multiple intermolecular hydrogen bonds in the most stable complexes.</jats:p>