Synthesis and Biochemical Evaluation of an Artificial, Fluorescent Glucosinolate (GSL)

Article abstract of DOI:10.1002/cbic.201900148

The synthesis of the first example of a fluorescent glucosinolate (GSL)–BODIPY conjugate based on an azide-containing artificial GSL precursor (GSL-N₃) is reported. Biochemical evaluation of the artificial GSLs revealed that the compounds are converted to the corresponding isothiocyanates in the presence of myrosinase. Furthermore, myrosinase-catalyzed hydrolysis in the presence of plant specifier proteins yielded the expected alternative products, namely nitriles. The easy assembly of the fluorescent GSL–BODIPY conjugate by click chemistry from GSL-N₃ holds potential for application as a fluorescence labeling tool to investigate GSL-associated processes.

Full text of DOI:10.1002/cbic.201900148

Accepted Article
Title: Synthesis and biochemical evaluation of an artificial, fluorescent
glucosinolate (GSL)
Authors: Carina Patrizia Glindemann, Anita Backenköhler, Matthias
Strieker, Ute Wittstock, and Philipp Klahn
This manuscript has been accepted after peer review and appears as an
Accepted Article online prior to editing, proofing, and formal publication
of the final Version of Record (VoR). This work is currently citable by
using the Digital Object Identifier (DOI) given below. The VoR will be
published online in Early View as soon as possible and may be different
to this Accepted Article as a result of editing. Readers should obtain
the VoR from the journal website shown below when it is published
to ensure accuracy of information. The authors are responsible for the
content of this Accepted Article.
To be cited as: ChemBioChem 10.1002/cbic.201900148
Link to VoR: http://dx.doi.org/10.1002/cbic.201900148
A Journal of
www.chembiochem.org

ChemBioChem
10.1002/cbic.201900148
COMMUNICATION
Synthesis and biochemical evaluation of an artificial, fluorescent
glucosinolate (GSL)
[a]
[b]
[b]
[b]
Carina Patrizia Glindemann, Anita Backenköhler, Matthias Strieker, Ute Wittstock,
Klahn*[a]
and Philipp
of the isothiocyanates, e.g. chemoprotective,[1,2,4,20–22] and
Abstract: The synthesis of the first example of a fluorescent
glucosinolate-BODIPY conjugate (GSL-BODIPY) based on an azide
antibacterial effects.[
1,2,4,23]
. The bioactivities are related to the
reaction of isothiocyanates with biological nucleophiles such as
amino- and sulfhydryl moieties of enzymes.[ While humans
possess no thioglucosidases in their enzyme portfolio, it has been
shown that several bacteria of the gut microbiome possess
thioglucosidase activity enabling them to degrade GSLs and
release isothiocyanates.[
3
containing artificial GSL precursor (GSL-N ) is reported. The
24]
biochemical evaluation of the novel artificial GSLs revealed that the
compounds are converted to the corresponding isothiocyanates in the
presence of myrosinase. Furthermore, myrosinase-catalyzed
hydrolysis in the presence of plant specifier proteins yielded the
expected alternative products, namely nitriles. The easy assembly of
the fluorescent GSL-BODIPY conjugate via click chemistry from GSL-
1,25]
In the context of studies on GSL metabolism and transport in
plants, herbivores, bacteria or humans, artificial fluorescent GSLs,
which release
isothiocyanates
as nucleophile-reactive
3
N holds potential for the application as fluorescence labeling tool for
fluorophores in the presence of thioglucosidases can serve as
valuable tools in fluorescence imaging. Additionally, such
compounds could be utilized for the fluorescence detection of
thioglucosidase-producing bacteria. Due to their interesting
the investigation of GSL-associated processes.
Glucosinolates (GSLs) are secondary metabolites produced by
plants of the order Brassicales including several agricultural crops
of the Brassicaceae such as cauliflower, radish, white and black
mustard, broccoli or rocket. They are part of the myrosinase-GSL
defense system that protects against herbivores (Scheme 1).[1–4]
Chemically, GSLs are thioglycosidic thiohydroximate-O-
sulfonates with variable, amino acid-derived side chains, which
are stored in the vacuole of so-called S-cells by the producing
plants.[ Adjacent myrosin cells contain the enzyme myrosinase
biological activities natural GSLs have been targeted by several
total syntheses.[
26–32]
Additionally, the syntheses of several
[
31–33]
[34–
artificial GSLs bearing non-natural
or isotopically labelled
3
8]
[39,40]
aglycones and glucose units as well as α-anomeric GSLs
have been reported. Very recently, Tatibouët and co-workers
reported a mannoside-GSL glycoconjugate as labeling probe for
lectins.[
41]
Herein, we report the synthesis and biochemical
[42]
evaluation of the first
artificial, fluorescent GSL as molecular
5]
tool for fluorescence imaging of GSL-associated biological
processes.
[
6,7]
in vacuole-derived myrosin bodies . Myrosinases (thioglucoside
glucohydrolases, EC 3.2.1.147) hydrolyze the anomeric
thioglycosidic bond of GSLs upon tissue damage under release
of glucose and a thiohydroximate-O-sulfonate aglycone.[4] The
aglycone undergoes
a Lossen rearrangement to form a
corresponding isothiocyanante, which acts as toxic or deterrent
[
2–4]
defense compound.
Interestingly, myrosinases have also
been identified in certain insects.[8–10] Many plants of the
Brassicaceae possess specifier proteins as additional
components of the myrosinase-GSL system[11–13] In the presence
of these proteins, the aglycone is converted to less reactive
[
14,15]
[16,17]
alternative products such as nitriles,
thiocyanates
or
epithionitriles[
18]
whose function is not well understood.
Structurally different specifier proteins are used by some
specialist herbivores such as Pieris rapae to overcome the
myrosinase-GSL defense of their host plants.[19]
Besides their roles in plant defense, glucosinolates are thought to
provide health benefits to humans due to a variety of bioactivities
[
[
a]
b]
M. Sc. Carina, Patrizia Glindemann, Dr. Philipp Klahn*
ORC ID: 0000-0003-4713-2345
Institute of Organic Chemistry
Technische Universität Carolo Wilhelmina zu Braunschweig
Hagenring 30, 38106 Braunschweig (Germany)
E-mail: p.klahn@tu-braunschweig.de
Anita Backenköhler, Dr. Matthias Strieker, Prof. Dr. Ute Wittstock
ORC ID: 0000-0002-0914-8453
Institute of Pharmaceutical Biology
Technische Universität Carolo Wilhelmina zu Braunschweig
Mendelssohnstrasse 1, 38106 Braunschweig
E-mail: u.wittstock@tu-braunschweig.de
Scheme 1. Myrosinase-glucosinolate (GSL) defense system of plants of the
order Brassicales and GSL breakdown by myrosinase.
Supporting information for this article is given via a link at the end of
the document.
For internal use, please do not delete. Submitted_Manuscript
This article is protected by copyright. All rights reserved.

ChemBioChem
10.1002/cbic.201900148
COMMUNICATION
hydroxylamine 4 was obtained in 97% yield in a 1:1-mixture of E-
and Z-isomers. This mixture was converted to the chloro oxime 5
in the presence of N-chloro succinimide in DMF in quantitative
yield giving exclusively the Z-isomer, which was directly used in
the next step without any further purification. In parallel, 1-thio-β-
D-glucopyranose (7) was prepared from glucose (6) in 4 steps
adapted from literature known procedures.[
28,43]
Coupling of 1-
thio-β-D-glucopyranose (7) and the chloro oxime 5 in the presence
of triethylamine in THF led to the formation of the GSL precursor
8
in 57% yield. The treatment of 8 with an excess of sulfur trioxide
pyridine complex in the presence of pyridine in dichloromethane
at 60°C led to the formation of the corresponding thiohydroximate-
O-sulfonate, which was converted into its potassium salt Ac
GSL-N in the presence of aqueous potassium hydrogen
carbonate solution. Finally, after deacetylation in the presence of
methanolic ammonia solution the desired artificial GSL GSL-N
4
-
3
3
was obtained in quantitative yield. To demonstrate the loading
with alkyne-tagged fluorophores, we attached the BODIPY
fluorophore 9 (λEx = 480 nm, λEm = 535 nm) by copper(I)-mediated
azide-alkyne click chemistry obtaining artificial, fluorescent GSL-
BODIPY in 87% yield.
Scheme 2. Variable platform for the synthesis of artificial, fluorescent GSLs or
GSL hydrolysis products via azide-alkyne click approach based on GSL-N .
3
With GSL-N
these artificial GSLs are still accepted as substrates by plant
myrosinases. We incubated GSL-N with myrosinase (purified
from seeds of Sinapis alba (Brassicaceae)) in MES buffer at 22°C
for 10, 40 and 120 min. After addition of benzonitrile as an internal
standard, the aqueous samples were extracted with
dichloromethane and analyzed by GC-MS. As shown in Figure 1,
3
and GSL-BODIPY in hand, we next investigated if
In order to develop a variable platform for artificial, fluorescent
GSLs we envisaged to generate GSL-N (Scheme 2) bearing an
azide moiety for easy and fast attachment of different
fluorophores containing terminal or strained internal alkynes via
copper-mediated or copper-free azide-alkyne click chemistry,
respectively.
3
3
3
GSL-N was hydrolyzed in the presence of myrosinase leading to
Therefore, the chloro oxime 5 as activated precursor for the
aglycone was synthesized from commercially available 4-
chlorobutanol (1) in 4 steps as shown in Scheme 3. First the
nucleophilic substitution of the chlorine atom by sodium azide at
the formation of the corresponding isothiocyanate 10 identified by
its molecular mass ion 142 m/z (See SI, Figure S1, A). Detectable
amounts of isothiocyanate 10 were formed already after 10 min
(Figure 1 B). In the absence of myrosinase no formation of 10 was
observed (Figure 1 A). Substrate conversion followed Michaelis-
70°C in DMF gave azido alcohol 2 in 89% yield.
Menten kinetics with a K
m
of 888 ± 143 µM and a Kcat of 37.9 s-1
(
Figure 2), i.e. values within the range determined with natural
[
44,45]
GSLs.
Figure 1. Isothiocyanate formation upon hydrolysis of GSL-N
GSL-N (2 mM) was incubated in 50 mM MES buffer (pH 6) in the absence (A)
or presence (B-D) of purified myrosinase from S. alba at 22°C. Samples were
extracted with CH Cl after 10 min (B), 40 min (C), or 120 min (A, D), and
3
by myrosinase.
3
3
Scheme 3. Synthesis of GSL-N and GSL-BODIPY.
2
2
extracts were analyzed by GC-MS. Total ion chromatograms (TIC) are shown.
IS: internal standard (benzonitrile). Peak identities were confirmed by high-
resolution mass spectrometry (See SI, Figures S1 A-B).
Oxidation in the presence of IBX led to the formation of the azido
aldehyde 3 in 80% yield. By treatment of 3 with hydroxylamine
hydrochloride in the presence of sodium acetate the
For internal use, please do not delete. Submitted_Manuscript
This article is protected by copyright. All rights reserved.

ChemBioChem
10.1002/cbic.201900148
COMMUNICATION
was no longer formed in favour of nitrile 11 (See SI, Figure S2).
Thiocyanate-forming protein from Thlaspi arvense (Brassicaceae;
TaTFP) was also able to promote nitrile formation upon hydrolysis
of GSL-N yielding 11. In this case, 30 µg TaTFP were not
3
sufficient to prevent formation of 10. This has also been observed
for conversion of its natural substrate, allylglucosinolate
[
46]
aglycone. Considering that both, 10 and 11, present an azide
function readily available for click chemistry, makes GSL-N an
3
attractive probe for the investigation of GSL degradation and
metabolism in plants.
The results of the hydrolysis experiments with GSL-BODIPY in
the presence of myrosinase were less straight forward as initial
GC-MS analyses failed to identify the expected BODIPY-
isothiocyanate 12 within dichloromethane extracts of the reaction
mixture. However, the LC-MS-based analysis of the fluorescent
aqueous layers (See SI, Figure S3) led to the identification of the
desired isothiocyanate 12 by its molecular mass ion 543 m/z (ESI,
+
[
M[12]+Na] , Figure
4
and SI, Figure S4 A). To further
substantiate our finding, we treated 12 purified from the aqueous
layer with aqueous ammonia solution and were able to identify the
expected thiourea product 14 with a molecular mass of 560 m/z
+
(
ESI, [M[14]+Na] , see SI, Figure S4, C).
Figure 2. Myrosinase kinetics with artificial glucosinolates as substrates. GSL-
N or GSL-BODIPY (25-2500 µM) was incubated with purified myrosinase from
3
S. alba in 50 mM Tris HCl (pH 7.5) at 25°C. Substrate conversion and product
formation were monitored by HPLC. Non-linear regression was applied using
the Michaelis-Menten equation. Means ± SD are shown (N=3).
Figure 3. Nitrile formation upon hydrolysis of GSL-N
3
by myrosinase in the
presence of specifier proteins. GSL-N (2 mM) was incubated with purified
3
myrosinase from S. alba in 50 mM MES buffer (pH 6) in the absence (A) or
presence of AtNSP3 (10 µg; B) or TaTFP (30 µg; C) at 22°C for 120 min.
Samples were extracted with CH Cl , and extracts were analyzed by GC-MS.
2 2
Total ion chromatograms (TIC) are shown. IS: internal standard (benzonitrile).
Peak identities were confirmed by high-resolution mass spectrometry (See SI,
Figures S1 A-B).
Figure 4. Isothiocyanate formation upon hydrolysis of GSL-BODIPY by
myrosinase. GSL-BODIPY (2 mM) was incubated in 50 mM MES buffer (pH 6)
in the absence (A) or presence (B-D) of purified myrosinase from S. alba at
22°C. Aliquots were taken from the reaction mixture after 10 min (B), 40 min (C),
or 120 min (A, D) and analyzed by HPLC. The peak at 4.87 min from (D) was
collected and analyzed by HPLC directly (E) or after reaction with NH OH to
4
yield the thiourea derivative (F). Chromatograms recorded at λ= 498 nm are
shown. Peak identities were confirmed by high-resolution mass spectrometry
Next, we tested if GSL-N
formation by purified plant specifier proteins heterologously
expressed in Escherichia coli. The incubation of GSL-N with
3
hydrolysis can be diverted to nitrile
3
myrosinase and 10 µg nitrile-specifier protein from Arabidopsis
thaliana (Brassicaceae; AtNSP3) led to the formation of the
corresponding nitrile 11 (Figure 3 B), identified by its molecular
(See SI, Figures S4 A-C).
mass ion 110 m/z (See SI, Figure S1, B), indicating that GSL-N
3
aglycone can serve as substrate for specifier proteins. In the
presence of 30 µg AtNSP3, the corresponding isothiocyanate 10
For internal use, please do not delete. Submitted_Manuscript
This article is protected by copyright. All rights reserved.

ChemBioChem
10.1002/cbic.201900148
COMMUNICATION
In contrast to the hydrolysis of GSL-N
significant amounts of the corresponding nitrile 13 were also
formed during hydrolysis of GSL-BODIPY (Figure 4, B-D) as
confirmed by its molecular mass ion 511 m/z (ESI, [M[13]+Na] ,
see SI, Figure S4 B).
3
and natural GSLs,
Keywords: Glucosinolates • Thioglucosidases • Isothiocyanates
•
Fluorescence labelling • artificial natural product derivatives
+
[
1] F. S. Hanschen, E. Lamy, M. Schreiner, S. Rohn, Angew. Chem.
Int. Ed. 2014, 53, 11430–11450.
Product formation followed Michaelis-Menten kinetics with a K
m
of
1
4
64 ± 47 µM and a Kcat of 2.9 s- (Figure 2), i.e. about tenfold lower
[2]
K. G. Ramawat, J.-M. Mérillon, Eds. , Glucosinolates, Springer,
2017.
3
efficiency than product formation from GSL-N , but still in the
range reported with natural GSLs. When myrosinase-catalyzed
hydrolysis was performed in presence of specifier protein AtNSP3
no significant amounts of the nitrile 13 were formed, instead the
overall hydrolysis was slower (See SI, Figure S5). As a possible
explanation, AtNSP3 might block the binding pocket of
myrosinase without being able to accept the aglycone of GSL-
BODIPY due to its size. Very small amounts of 13 were also
formed in absence of myrosinase (Figure 4, A). This slow auto-
degradative process is currently not fully understood.
[3]
U. Wittstock, B. A. Halkier, Trends Plant Sci. 2002, 7, 263–270.
[
[
[
4]
5]
6]
S. Kopriva, Ed. , Glucosinolates: Advances in Botanical
Research, Academic Press, London, 2016.
O. A. Koroleva, A. Davies, R. Deeken, M. R. Thorpe, A. D.
Tomos, R. Hedrich, Plant Physiol. 2000, 124, 599–608.
R. Kissen, J. T. Rossiter, A. M. Bones, Phytochem. Rev. 2009,
8, 69–86.
[7]
[8]
P. Romero, S. Zaidi, A. K. Dunker, Proc. 13th Int. Congr. Genes,
Gene Fam. Isozymes 2005, 7–13.
In summary, we synthesized the first artificial, fluorescent GSL-
derivative as well as an artificial, azido-functionalized GSL. We
demonstrated their ability to serve as substrate for myrosinase
F. Beran, Y. Pauchet, G. Kunert, M. Reichelt, N. Wielsch, H.
Vogel, A. Reinecke, A. Svato , I. Mewis, D. Schmid, et al., Proc.
Natl. Acad. Sci. 2014, 111, 7349–7354.
and, in case of GSL-N
Therefore, we consider GSL-N
3
, as substrate for specifier proteins.
and GSL-BODIPY suitable
3
[
[
9]
A. M. E. Jones, M. Bridges, A. M. Bones, R. Cole, J. T. Rossiter,
Insect Biochem. Mol. Biol. 2001, 31, 1–5.
probes for tracing GSLs and their metabolism in biological
systems.
10] B. Pontoppidan, B. Akborn, S. Eriksson, J. Meijer, Eur. J.
Biochem. 2001, 268, 1041–1048.
[
[
[
11] U. Wittstock, M. Burow, IUBMB Life 2007, 59, 744–751.
Experimental Section
12] U. Wittstock, M. Burow, The Arabidopsis Book 2010, 8, e0134.
13] D. Eisenschmidt‐Bönn, N. Schneegans, A. Backenköhler, U.
Wittstock, W. Brandt, Plant J. 2019, DOI:10.1111/tpj.14327.
The Experimental Details can be found in the Supporting Information.
[
[
14] R. Kissen, A. M. Bones, J. Biol. Chem. 2009, 284, 12057–12070.
15] M. Burow, A. Losansky, R. Mueller, A. Plock, D. J. Kliebenstein,
Author’s Contributions
U. Wittstock, Plant Physiol. 2009, 149, 561–574.
[
16] J. C. Kuchernig, A. Backenköhler, M. Lübbecke, M. Burow, U.
The research was conceived by P.K.. The manuscript was written
by P.K. with contributions from U.W.. All compounds were
synthesized by C.P.G., and P.K.. Biochemical evaluation of the
compounds was planned by U.W., A.B., and M.S. and conducted
by A.B. and M.S.. / All authors have given approval to the final
version of the manuscript.
Wittstock, Phytochemistry 2011, 72, 1699–1709.
[17] M. Burow, A. Bergner, J. Gershenzon, U. Wittstock, Plant Mol.
Biol. 2007, 63, 49–61.
[18] V. Lambrix, M. Reichelt, T. Mitchell-Olds, D. J. Kliebenstein, J.
Gershenzon, Plant Cell 2001, 13, 2793–2807.
[
19] U. Wittstock, N. Agerbirk, E. J. Stauber, C. E. Olsen, M. Hippler,
T. Mitchell-Olds, J. Gershenzon, H. Vogel, Proc. Natl. Acad. Sci.
U. S. A. 2004, 101, 4859–4864.
[
[
[
20] J. V. Higdon, B. Delage, D. E. Williams, R. H. Dashwood,
Conflict of interests
Pharmacol. Res. 2007, 55, 224–236.
21] J. R. Mays, R. L. W. Roska, S. Sarfaraz, H. Mukhtar, S. R.
There are no conflicts of interests to declare.
Rajski, ChemBioChem 2008, 9, 729–747.
22] E. Elhalem, R. Recio, S. Werner, F. Lieder, J. M. Calderón-
Montanõ, M. López-Lázaro, I. Fernández, N. Khiar, Eur. J. Med.
Chem. 2014, 87, 552–563.
Acknowledgements
[
[
[
[
[
23] L. Romeo, R. Iori, P. Rollin, P. Bramanti, E. Mazzon, Molecules
2018, 23, 624.
This work has been carried out within the framework of the
SMART BIOTECS alliance between the Technische Universität
Braunschweig and the Leibniz Universität Hannover. This
initiative is supported by the Ministry of Science and Culture
24] P. Chan, J. A. Uchizono, Essentials Pharmacol. Anesth. Pain
Med. Crit. Care 2015, 2532, 3–47.
25] J. R. K. Cairns, A. Esen, Cell. Mol. Life Sci. 2010, 67, 3389–
3405.
(
MWK) of Lower Saxony, Germany. P.K. thanks Fonds der
26] S. Y. Amazoe, K. H. Asegawa, H. S. Higemori, Biosc.
Biotechnol. Biochem. 2009, 73, 785–787.
Chemischen Industrie for their financial support. The content of
this work is solely the responsibility of the authors and does not
necessarily represent the official views of the funding agencies.
The authors thank the mass spectrometry unit of the Institute of
Organic Chemistry at the TU Braunschweig, in particular Dr.
Ulrich Papke and Dr. Till Beuerle, for analytical support as well as
Robert Zscherp and Dr. Anna Luisa Klahn for helpful discussion
and proofreading of the manuscript.
27] D. Cerniauskaite, J. Rousseau, A. Sackus, P. Rollin, A.
Tatibouët, European J. Org. Chem. 2011, 2293–2300.
[28] W. Abramski, M. Chmielewski, J. Carbohydr. Chem. 2006, 15,
109–113.
[29] M. S. C. Pedras, Q. H. To, G. Schatte, Chem. Commun. 2016,
5
2, 2505–2508.
[30] M. Mavratzotis, S. Cassel, S. Montaut, P. Rollin, Molecules
018, 23, 1–15.
2
For internal use, please do not delete. Submitted_Manuscript
This article is protected by copyright. All rights reserved.

ChemBioChem
10.1002/cbic.201900148
COMMUNICATION
[
[
[
[
[
[
[
[
[
[
31] Q. V. Vo, C. Trenerry, S. Rochfort, J. Wadeson, C. Leyton, A.
A. Mechler, Carbohydr. Res. 2018, 455, 45–53.
B. Hughes, Bioorg. Med. Chem. 2013, 21, 5945–5954.
[
41] G. Cutolo, F. Reise, M. Schuler, R. Nehmé, G. Despras, J.
Brekalo, P. Morin, P. Y. Renard, T. K. Lindhorst, A. Tatibouët,
Org. Biomol. Chem. 2018, 16, 4900–4913.
32] Y. W. Lim, M. J. H. Ong, R. J. Hewitt, Synthesis 2018, 50, 1640–
1
650.
33] N. E. Davidson, T. J. Rutherford, N. P. Botting, Carbohydr. Res.
001, 330, 295–307.
34] J. J. Morrison, N. P. Botting, J. Label. Compd. Radiopharm.
005, 48, 897–907.
[42] During revision of the present work a similar approach for
artificial, fluorescent GSLs was published: C. Sabot, J. W. Fredy,
G. Cutolo, B. Poret, R. Nehmé, M. Hubert-Roux, P. Gandolfo,
H. Castel, M. Schuler, A. Tatibouët, et al., Bioconjug. Chem.
2
2
2
019, acs.bioconjchem.9b00153.
43] P. Shu, J. Zeng, J. Tao, Y. Zhao, G. Yao, Q. Wan, Green Chem.
015, 17, 2545–2551.
44] I. Braschi, O. Leoni, S. Cinti, S. Palmieri, C. E. Gessa, Plant Soil
011, 339, 209–218.
35] N. P. Botting, A. A. B. Robertson, J. J. Morrison, J. Label.
Compd. Radiopharm. 2007, 50, 260–263.
[
[
2
36] J. T. Rossiter, J. A. Pickett, M. H. Bennett, A. M. Bones, G.
Powell, J. Cobb, Phytochemistry 2007, 68, 1384–1390.
2
37] M. S. C. Pedras, Q. H. To, J. Label. Compd. Radiopharm. 2018,
[
[
45] “www.brenda-enzymes.org,” 2019.
6
1, 94–106.
38] Q. Zhang, T. Lebl, A. Kulczynska, N. P. Botting, Tetrahedron
009, 65, 4871–4876.
46] F. Gumz, J. Krausze, D. Eisenschmidt, A. Backenköhler, L.
Barleben, W. Brandt, U. Wittstock, Plant. Mol. Biol. 2015, 89,
2
67–81.
39] M. Blanc-Muesser, H. Driguez, B. Joseph, M. C. Viaud, P. Rollin,
Tetrahedron Lett. 1990, 3867–3868.
40] Q. V. Vo, S. Rochfort, P. C. Nam, T. L. Nguyen, T. T. Nguyen,
For internal use, please do not delete. Submitted_Manuscript
This article is protected by copyright. All rights reserved.

ChemBioChem
10.1002/cbic.201900148
COMMUNICATION
Entry for the Table of Contents
COMMUNICATION
C. P. Glindemann, A. Backenköhler, M.
Strieker, U. Wittstock, and P. Klahn*
Page No. – Page No.
Synthesis and biochemical evaluation
of an artificial, fluorescent gluco-
sinolate (GSL)
From mustard into the fluorescent marker toolbox: Synthesis and biochemical
evaluation of a platform compound for the generation of artificial, fluorescent
glucosinolates (GSLs).
For internal use, please do not delete. Submitted_Manuscript
This article is protected by copyright. All rights reserved.