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Page 34
allied
academies
February 18-19, 2019 | Paris, France
Joint Event
Green Chemistry and Technology
8th World Congress on International Conference on
Organic and Inorganic Chemistry
Journal of Industrial and Environmental Chemistry| Volume: 3
A new artificial imine reductase based on dalbapeptides metal interaction
Isabella Rimoldi
University of Milan, Italy
Homogeneous catalysis by transitionmetals containing chiral
bidentate ligands has beenoften considereda valid strategy
to obtain high productivity, stereoselectivity and atomeconomy
by many academic and industrial researchers interested in the
synthesis of optically pure compounds. The same attraction
has been reserved to enzymatic catalysis based on the fact
that biocatalysis has many benefits to offer in the context of
green chemistry. Considering the ability of macromolecules to
selectively discriminate substrates and the number of chemical
transformations catalyzed by transition metals, which have
not been observed to occur enzymatically, in the last decade
several research groups reasoned that a hybrid catalyst may
combine some of the most attractive features of metal and
enzymatic catalysts. In this contest, the use of a dalbapeptides,
such as vancomycin, teicoplanin, ristocetin etc, could be an
interesting alternative to the well-known biotin/(strept)avidin
system. Dalbapeptides are known for their strong antibacterial
activity due to their interaction with the dimer D-Ala-D-Ala in
the terminal chain of bacterial cell wall peptidoglycan with a
dissociation constant KD = ~10-17 M and they have recently
been investigated for their capability to interact with different
transition metals such as copper. By exploiting these features
of the class of glycopeptides, new hybrid iridium systems
were prepared and evaluated as catalysts in asymmetric
transfer hydrogenation of different cyclic imine substrates
chosen for their important applications in medicinal chemistry.
e:
J Ind Environ Chem 2019, Volume 3
DOI: 10.4066/2591-7331-C1-009
Notes: