Hydrophobic interactions affect hydrogen bond strengths in complexes between peptides and vancomycin or ristocetin.
A study on complexes of the glycopeptide antibiotics vancomycin and ristocetin with various dipeptides and tripeptides shows that the intermolecular hydrogen bond strengths of the complexes are reasonably well correlated with their free energy of formation. Such correlation is not anticipated on the basis of a purely hydrophobic interaction of the peptide side-chains with the antibiotics. It is also shown that the free energy changes observed are very different from those expected as a result of hydrophobic forces. These facts suggest that addition of a hydrophobic group not only allows hydrophobic bonding but also strengthens existing hydrogen bonds. The increased hydrogen bond strength can be an important factor in determining the overall binding energy.
D001665:Binding Sites; D006860:Hydrogen Bonding; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D012310:Ristocetin / Q000378:metabolism*; D013816:Thermodynamics; D014640:Vancomycin / Q000378:metabolism*
D010455:Peptides; D012310:Ristocetin; D014640:Vancomycin