The article describes an NMR spectroscopy study of interactions between vancomycin
and a muramyl pentapeptide in two complexes: vancomycin and a native muramyl pentapeptide
ended with D-alanine (MPP-D-Ala), and vancomycin and a modified muramyl pentapeptide ended
with D-serine (MPP-D-Ser). The measurements were made in a 9:1 mixture of H2O and D2O. The
obtained results confirmed the presence of hydrogen bonds previously described in the literature. At
the same time, thanks to the pentapeptide model used, we were able to prove the presence of two
more hydrogen bonds formed by the side chain amino group of L-lysine and oxygen atoms from
the vancomycin carboxyl and amide groups. This type of interaction has not been described before.
The existence of these hydrogen bonds was confirmed by the 1H NMR and molecular modeling.
The formation of these bonds incurs additional through-space interactions, visible in the NOESY
spectrum, between the protons of the L-lysine amino group and a vancomycin-facing hydrogen atom
in the benzylic position. The presence of such interactions was also confirmed by molecular dynamics
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