Bioorganic & Medicinal Chemistry Letters
Towards new antibiotics targeting bacterial transglycosylase: Synthesis
of a Lipid II analog as stable transition-state mimic inhibitor
Xiaolei Wang a, Larissa Krasnova a, Kevin Binchia Wu a, Wei-Shen Wu b, Ting-Jen Cheng b,
Chi-Huey Wong a,b,
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a The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92122, USA
b Genomics Research Center, Academia Sinica, 128 Sec 2 Academia Road, Taipei, Nankang 115, Taiwan
a r t i c l e i n f o
a b s t r a c t
Article history:
Described here is the asymmetric synthesis of iminosugar 2b, a Lipid II analog, designed to mimic the
transition state of transglycosylation catalyzed by the bacterial transglycosylase. The high density of
functional groups, together with a rich stereochemistry, represents an extraordinary challenge for chem-
ical synthesis. The key 2,6-anti- stereochemistry of the iminosugar ring was established through an irid-
ium-catalyzed asymmetric allylic amination. The developed synthetic route is suitable for the synthesis
of focused libraries to enable the structure–activity relationship study and late-stage modification of imi-
nosugar scaffold with variable lipid, peptide and sugar substituents. Compound 2b showed 70% inhibition
of transglycosylase from Acinetobacter baumannii, providing a basis for further improvement.
Ó 2018 Elsevier Ltd. All rights reserved.
Received 23 January 2018
Revised 12 March 2018
Accepted 13 March 2018
Available online xxxx
Keywords:
Iminosugar
Inhibitor
Lipid II
Transglycosylase
Synthesis
Introduction
identified (e.g., vancomycin), the direct binders of TG with potent
inhibitory activities and pharmacological properties suitable for
The increasingly common occurrences of infections caused by
the drug-resistant bacteria represent a major threat to public
health.1 The urgent demand for novel antibacterials has led to
the search for underexploited drug targets. In the past, targeting
the assembly of peptidoglycan (PG), a polymer-like structure that
helps maintain the integrity of bacteria cell and protects it from
lysis, has proven to be a successful strategy for the discovery of
antibiotics. Our group has a long-standing interest in the enzyme
transglycosylase (TG) as target, which catalyzes the polymerization
of Lipid II (1, Fig. 1A) to generate a nascent PG before it is cross-
linked by transpeptidase (Fig. 1B). First reported 50 years ago,2a
TG is still viewed as a difficult,2b albeit an attractive target.2c,2d
Located on the external surface of the cytoplasmic membrane, TG
is accessible to potential inhibitors. As TG does not have any
mammalian counterpart, it is possible to design new antibiotics
that are specific against prokaryotic pathogens. In addition,
because TG recognizes an invariant carbohydrate backbone, it
may be less susceptible to the traditional mechanisms of
resistance development.3 Although, antibacterials that inhibit Lipid
II polymerization by sequestering its substrate have been
clinical use have yet to be developed. One major effort in this
direction has been the optimization of moenomycin structure,4
the only TG-specific inhibitor known to date.
Based on recent efforts towards finding the minimal required
features of Lipid II/Lipid IV,5–7 we designed structure 2 (Fig. 1A)
as a potential transition-state mimic of the TG-catalyzed reaction.5
Compound 2 consists of iminosugar ring connected to an addi-
tional ring of GlcNAc, a truncated peptide moiety with two essen-
tial methyl groups from the lactyl-alanine sequence,5a,6a,6d along
with
a
phosphono-phosphate linked lipid chain,6b which is
necessary for the proper recognition and binding. Towards
structure 2, our group has initially reported the synthesis of the
truncated analog 2a (Fig. 1A), which indeed showed inhibition of
TG function.6b The two drawbacks of compound 2a are of note.
First, because TG is a processive enzyme,7 it is highly unlikely that
this mono-sugar derivative 2a can reach the desired donor site of
TG due to the lack of the second GlcNAc, therefore preventing
enzyme to process 2a. Hence, the observed activity could be a
result of 2a binding to the acceptor site only, and its designation
as a transition-state analog inhibitor could not be fully realized.
Second, the synthetic strategy developed for the assembly of 2a
is not suitable for the preparation of the highly functionalized imi-
nosugar 2 and its derivatives,6b required for the detailed structure–
activity relationship (SAR) study of TG inhibition. To solve the
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Corresponding author at: Genomics Research Center, Academia Sinica, 128 Sec
2 Academia Road, Taipei, Nankang 115, Taiwan.
0960-894X/Ó 2018 Elsevier Ltd. All rights reserved.