The stereochemical course of 2-methylisoborneol biosynthesis

• Binbin Gu,
• Anwei Hou and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2022, 18, 818–824, doi:10.3762/bjoc.18.82

• Binbin Gu Anwei Hou Jeroen S. Dickschat Kekulé-Institute of Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Straße 1, 53121 Bonn, Germany 10.3762/bjoc.18.82 Abstract Both enantiomers of 2-methyllinalyl diphosphate (2-Me-LPP) were synthesized enantioselectively using

• resulted in a biosynthetic model that includes the methylation of geranyl diphosphate (GPP) to 2-methyl-GPP (2-Me-GPP), followed by cyclization to compound 1 (Scheme 1A) [8]. This process involves the isomerization of 2-Me-GPP by allylic transposition of diphosphate to 2-methyllinalyl diphosphate (2-Me-LPP

• biosynthesis of 1 can also be reconstituted in vitro through coupling of dimethylallyl diphosphate (DMAPP) with 2-methyl-IPP (2-Me-IPP; IPP = isopentenyl diphosphate) to 2-Me-GPP using farnesyl diphosphate synthase (FPPS), followed by cyclization through 2MIBS to 1 [26]. A recently described methyltransferase

Identification of the new prenyltransferase Ubi-297 from marine bacteria and elucidation of its substrate specificity

• Jamshid Amiri Moghaddam,
• Huijuan Guo,
• Karsten Willing,
• Thomas Wichard and
• Christine Beemelmanns

Beilstein J. Org. Chem. 2022, 18, 722–731, doi:10.3762/bjoc.18.72

• homogentisate and geranylgeranyl diphosphate [10][11]. Another intriguing Ptase, called AuaA, has been reported to catalyze the farnesylation of 2-methyl-4-hydroxyquinoline using farnesyl diphosphate (FPP), which results in the metabolite aurachin D [12][13]. Following up on our recent exploration of the

The enzyme mechanism of patchoulol synthase

• Houchao Xu,
• Bernd Goldfuss,
• Gregor Schnakenburg and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2022, 18, 13–24, doi:10.3762/bjoc.18.2

• of an unexpected rearrangement this structural assignment was still erroneous, and the correct structure 3 was finally established by X-ray analysis of its chromic acid diester [6]. The patchoulol synthase (PTS) has been purified from plant leaves and shown to convert farnesyl diphosphate (FPP) into

• S3). Using dimethylallyl diphosphate (DMAPP) and (E)- and (Z)-(4-13C,4-2H)isopentenyl diphosphate (IPP) [18] in conjunction with FPP synthase (FPPS) from Streptomyces coelicolor [19] and PTS (Supporting Information File 1, Figure S11), stereogenic centres of known configuration are introduced at the

• isopentenyl diphosphate isomerase (IDI) from E. coli [20][21], FPPS, and PTS (Figure S12 in Supporting Information File 1). The additional 13C-labellings in these experiments serve for a sensitive monitoring of deuterium incorporation through HSQC spectroscopy. All X-ray and labelling experiments confirmed

Targeting active site residues and structural anchoring positions in terpene synthases

• Anwei Hou and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2021, 17, 2441–2449, doi:10.3762/bjoc.17.161

• mechanisms; isotopes; site-directed mutagenesis; terpenes; Introduction Terpenoids now span more than 90,000 known compounds, which makes them by far the largest class of natural products [1]. Despite this fact, all compounds are made from only two C5 building blocks, dimethylallyl diphosphate (DMAPP) and

• isopentenyl diphosphate (IPP), that can be fused by oligoprenyl diphosphate synthases to yield geranyl diphosphate (GPP, C10) as the precursor to monoterpenes, farnesyl diphosphate (FPP, C15) as sesquiterpene precursor, geranylgeranyl diphosphate (GGPP, C20) towards diterpenes, and geranylfarnesyl diphosphate

• (GFPP, C25) for sesterterpene biosynthesis. Type I terpene synthases (TPSs) activate these acyclic molecules by the abstraction of diphosphate to produce a reactive allyl cation that can initiate a cascade reaction through typical carbocation chemistry, including cyclisation reactions by intramolecular

Volatile emission and biosynthesis in endophytic fungi colonizing black poplar leaves

• Christin Walther,
• Pamela Baumann,
• Katrin Luck,
• Beate Rothe,
• Peter H. W. Biedermann,
• Jonathan Gershenzon,
• Tobias G. Köllner and
• Sybille B. Unsicker

Beilstein J. Org. Chem. 2021, 17, 1698–1711, doi:10.3762/bjoc.17.118

• culture and showed that both species are able to produce sesquiterpenes like (E)-β-farnesene (2), α- and β-chamigrene (4), and germacrene D [41]. In general, terpenes are derived from the five-carbon intermediates dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP), which are both produced

• by the mevalonate pathway in fungi [42]. The condensation of DMAPP with varying numbers of IPP residues results in products of various chain lengths: geranyl diphosphate (GPP, C10), farnesyl diphosphate (FPP, C15), and geranylgeranyl diphosphate (GGPP, C20). Terpene synthases (TPS) then convert the

On the mass spectrometric fragmentations of the bacterial sesterterpenes sestermobaraenes A–C

• Anwei Hou and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2020, 16, 2807–2819, doi:10.3762/bjoc.16.231

• enzymatic conversion of the correspondingly 13C-labelled isoprenyl diphosphate precursors with the sestermobaraene synthase from Streptomyces mobaraensis. The main compounds sestermobaraenes A, B, and C were analysed by gas chromatography–mass spectrometry (GC–MS), allowing for a deep mechanistic

• bacteria, that is characterised by an aspartate-rich motif (DDXXD) and an NSE triad (NDLXSXXXE) for binding of a trinuclear Mg2+ cluster [2][3]. The Mg2+ cations in turn bind to the diphosphate moiety of an isoprenoid diphosphate precursor and cause substrate ionisation by a diphosphate abstraction to

• isotopomers of (13C)geranylfarnesyl diphosphate (GFPP) were enzymatically prepared from the correspondingly labelled geranyl diphosphate (GPP), farnesyl diphosphate (FPP), geranylgeranyl diphosphate (GGPP), and isopentenyl diphosphate (IPP) with geranylfarnesyl diphosphate synthase (GFPPS) and then converted

Optical detection of di- and triphosphate anions with mixed monolayer-protected gold nanoparticles containing zinc(II)–dipicolylamine complexes

• Lena Reinke,
• Julia Bartl,
• Marcus Koch and
• Stefan Kubik

Beilstein J. Org. Chem. 2020, 16, 2687–2700, doi:10.3762/bjoc.16.219

• /bjoc.16.219 Abstract Gold nanoparticles covered with a mixture of ligands of which one type contains solubilizing triethylene glycol residues and the other peripheral zinc(II)–dipicolylamine (DPA) complexes allowed the optical detection of hydrogenphosphate, diphosphate, and triphosphate anions in

• depended on the nature of the anion, with diphosphate and triphosphate inducing visual changes at significantly lower concentrations than hydrogenphosphate. In addition, the sensing sensitivity was also affected by the ratio of the ligands on the nanoparticle surface, decreasing as the number of

• immobilized zinc(II)–dipicolylamine groups increased. A nanoparticle containing a 9:1 ratio of the solubilizing and the anion-binding ligand showed a color change at diphosphate and triphosphate concentrations as low as 10 μmol/L, for example, and precipitated at slightly higher concentrations

Synthesis of monophosphorylated lipid A precursors using 2-naphthylmethyl ether as a protecting group

• Jundi Xue,
• Ziyi Han,
• Gen Li,
• Khalisha A. Emmanuel,
• Cynthia L. McManus,
• Qiang Sui,
• Dongmian Ge,
• Qi Gao and
• Li Cai

Beilstein J. Org. Chem. 2020, 16, 1955–1962, doi:10.3762/bjoc.16.162

• phosphorylated using tetrabenzyl diphosphate in the presence of lithium bis(trimethyl)silylamide (LHMDS) in THF at −78 °C [23] to afford the anomeric phosphate 23 exclusively as the α-anomer. Finally, global deprotection of 23 (benzyl phosphate, Nap ethers, and naphthylidene acetal) were accomplished by

• of 29 was phosphorylated using tetrabenzyl diphosphate in the presence of LHMDS in THF at −78 °C. Then finally global deprotection (hydrogenation over Pd-black) was carried out to remove the naphthylidene acetal, Nap ethers, and the benzyl phosphate groups in compound 30. By this route the target

Synthesis, docking study and biological evaluation of ᴅ-fructofuranosyl and ᴅ-tagatofuranosyl sulfones as potential inhibitors of the mycobacterial galactan synthesis targeting the galactofuranosyltransferase GlfT2

• Marek Baráth,
• Jana Jakubčinová,
• Zuzana Konyariková,
• Stanislav Kozmon,
• Katarína Mikušová and
• Maroš Bella

Beilstein J. Org. Chem. 2020, 16, 1853–1862, doi:10.3762/bjoc.16.152

• enzymes require an activated sugar donor uridine diphosphate (UDP)-Galf, which is synthesized from UDP-galactopyranose (UDP-Galp) by the enzyme UDP-Galp mutase [9] (Supporting Information File 1, Figure S1). The recently published GlfT2 X-ray structure with a UDP donor part [10] was used in the reaction

• Information File 1, Figure S3). A small movement was observed only for the diphosphate part due to the proper accommodation of the Galf moiety within the GlfT2 binding pocket. This suggested that the UDP-Galf docked binding pose was reliable and could be used as a reference for the docking of the studied

Understanding the role of active site residues in CotB2 catalysis using a cluster model

• Keren Raz,
• Ronja Driller,
• Thomas Brück,
• Bernhard Loll and
• Dan T. Major

Beilstein J. Org. Chem. 2020, 16, 50–59, doi:10.3762/bjoc.16.7

• reaction. The coordinates of the amino acids and the substrate GGPP were taken from the corresponding X-ray structure, with a resolution of 1.8 Å [42]. In this approach, geometry optimizations with the “Modredundant” keyword were performed, and the active site residues, diphosphate moiety, and magnesium

Synthesis of C-glycosyl phosphonate derivatives of 4-amino-4-deoxy-α-ʟ-arabinose

• Lukáš Kerner and
• Paul Kosma

Beilstein J. Org. Chem. 2020, 16, 9–14, doi:10.3762/bjoc.16.2

• ; lipopolysaccharide; Introduction Glycosyltransferases are important enzymes that accomplish the transfer of activated sugar phosphates onto their respective acceptor molecules [1]. In most cases, nucleotide diphosphate sugars serve as the reactive species, but lipid-linked diphosphate derivatives are equally

• and the glycosyl transfer have not been fully explored yet. Previously, Kline and co-workers reported on the synthesis of acetylated 4-azido-arabinose phosphate and uridine diphosphate (UDP) derivatives. In addition, a 4-aminophosphoamidate UDP derivative was also obtained [8]. Whereas these compounds

Bacterial terpene biosynthesis: challenges and opportunities for pathway engineering

• Eric J. N. Helfrich,
• Geng-Min Lin,
• Christopher A. Voigt and
• Jon Clardy

Beilstein J. Org. Chem. 2019, 15, 2889–2906, doi:10.3762/bjoc.15.283

• diphosphate (FPP, 9) or geranylgeranyl diphosphate (GGPP, 10, Figure 5a) [11][53]. Upon binding of the precursor, the TC undergoes conformational changes to seal the hydrophobic binding pocket [54]. This induced-fit mechanism locks the acyclic precursor into a defined, preorganized conformation that positions

• hosts, many E. coli hosts have been engineered to increase precursor supply, provide redox partners for CYP enzymes, and overproduce oligoprenyl diphosphate. As is the case for other natural product classes, off-target effects of heterologous host enzymes have been reported to alter terpenoid structures

• [116]. In some cases, bacterial TCs are able to accept oligoprenyl diphosphates with different lengths. Spata-13,17-diene (39) synthase is an extreme example that can convert FPP (9), GGPP (10), and geranylfarnesyl diphosphate (GFPP, 11) into sesquiterpenes, diterpenes, and sesterterpenes, respectively

Emission and biosynthesis of volatile terpenoids from the plasmodial slime mold Physarum polycephalum

• Xinlu Chen,
• Tobias G. Köllner,
• Wangdan Xiong,
• Guo Wei and
• Feng Chen

Beilstein J. Org. Chem. 2019, 15, 2872–2880, doi:10.3762/bjoc.15.281

• PpolyTPS4 were able to produce sesquiterpenes and monoterpenes from the respective substrates farnesyl diphosphate and geranyl diphosphate. By comparing the volatile profile of P. polycephalum plasmodia and the in vitro products of PpolyTPS1 and PpolyTPS4, it was concluded that most sesquiterpenoids emitted

• diverse VOCs, terpenoids are the largest group. Terpenoids are biosynthesized from two C5 diphosphate compounds isopentenyl diphosphate (IPP) and its isomer dimethylallyl diphosphate (DMAPP), which are produced by either the mevalonate (MVA) pathway or the methylerythritol phosphate (MEP) pathway [9][10

• ]. The MVA pathway is found in eukaryotes, archaea, and a few bacteria, and the MEP pathway is present in several photosynthetic eukaryotes and bacteria [11]. Isoprenyl diphosphate synthases (IDSs) catalyze the formation of prenyl diphosphates of various chain length [12]. After that, terpene synthases

Nanangenines: drimane sesquiterpenoids as the dominant metabolite cohort of a novel Australian fungus, Aspergillus nanangensis

• Heather J. Lacey,
• Cameron L. M. Gilchrist,
• Andrew Crombie,
• John A. Kalaitzis,
• Daniel Vuong,
• Peter J. Rutledge,
• Peter Turner,
• John I. Pitt,
• Ernest Lacey,
• Yit-Heng Chooi and
• Andrew M. Piggott

Beilstein J. Org. Chem. 2019, 15, 2631–2643, doi:10.3762/bjoc.15.256

• -type sesquiterpenoids from farnesyl diphosphate is proposed to proceed via the protonation-initiated mechanism (class II terpene synthases) [24], which is distinct from the ionisation-initiated mechanism (class I) terpene synthases, where a carbocation is generated by the release of a diphosphate group

• FE257_006542 contains both class I (DDxxD/E) and class II (DxDD, QW) terpene synthases, we propose that FE257_006542 is responsible for both the cyclisation into drimanyl diphosphate and the hydrolysis of the diphosphate into drim-8-ene-11-ol. We propose the next step in the pathway is hydroxylation at C-6 or

Current understanding and biotechnological application of the bacterial diterpene synthase CotB2

• Ronja Driller,
• Daniel Garbe,
• Norbert Mehlmer,
• Monika Fuchs,
• Keren Raz,
• Dan Thomas Major,
• Thomas Brück and
• Bernhard Loll

Beilstein J. Org. Chem. 2019, 15, 2355–2368, doi:10.3762/bjoc.15.228

• CotB2 from the open, inactive, to the closed, active conformation have been obtained in great detail, allowing us to draw detailed conclusions regarding the catalytic mechanism at the molecular level. Moreover, numerous alternative geranylgeranyl diphosphate cyclization products obtained by CotB2

• will focus particularly on bacterial diterpene synthases, in context with other sesqui- and ditperpene synthases of bacterial, fungal and plant origin. The initial step in diterpene biosynthesis (Figure 1) is the incremental condensation of dimethylallyl diphosphate (1) and isopentylen diphosphate (2

• ) [12] to the acyclic terpene synthase substrate geranylgeranyl diphosphate 3 (GGDP) [1][13][14][15][16]. Following initial substrate binding and folding in a product-like conformation, the cyclization reaction can be subdivided into three steps: (1) generation of a reactive allyl carbocation as a

Harnessing enzyme plasticity for the synthesis of oxygenated sesquiterpenoids

• Melodi Demiray,
• David J. Miller and
• Rudolf K. Allemann

Beilstein J. Org. Chem. 2019, 15, 2184–2190, doi:10.3762/bjoc.15.215

• engineering; terpenes; Introduction Amorphadiene synthase (ADS) from Artemisia annua is a key enzyme involved in the biosynthesis of the antimalarial sesquiterpene drug artemisinin (1) [1][2][3][4]. ADS catalyses the Mg2+-dependent conversion of farnesyl diphosphate (FDP, 2) to amorpha-4,11-diene (3) with

• high regio- and stereochemical control (Scheme 1) [5][6][7]. The carbocationic reaction mechanism of ADS involves an isomerisation to nerolidyl diphosphate (NDP, 4) followed by breakage of the carbon–oxygen bond to generate the allylic cation 5. This allows rotation around the C2–C3 bond and 1,6-ring

• exposing (E)-β-farnesene synthase to diphosphate 11 (Supporting Information File 1). Further support for the structure of the minor product came from the excellent agreement of the diagnostic 1H NMR signals of 21 (H1 (δH = 5.25, d, JH,H = 17.5 Hz), H1’ (δH = 5.06, d, JH,H = 11.0 Hz), H2 (δH = 6.38, dd, JH

Genome mining in Trichoderma viride J1-030: discovery and identification of novel sesquiterpene synthase and its products

• Xiang Sun,
• You-Sheng Cai,
• Yujie Yuan,
• Guangkai Bian,
• Ziling Ye,
• Zixin Deng and
• Tiangang Liu

Beilstein J. Org. Chem. 2019, 15, 2052–2058, doi:10.3762/bjoc.15.202

• synthases in Trichoderma viride have been seldom studied, despite the efficiency of filamentous fungi for terpenoid production. Using the farnesyl diphosphate-overexpressing Saccharomyces cerevisiae platform to produce diverse terpenoids, we herein identified an unknown sesquiterpene synthase from T. viride

• three types based on their amino acid sequence. Type I TPSs are metal-dependent enzymes that initiate cyclisation by the elimination of diphosphate groups from precursors and carbocation formation, and type II TPSs initiate the catalytic process by the protonation of an olefinic double bond [7]. The

• recently reported type III TPSs, UbiA-related TPSs, also catalyse cascade reactions by diphosphate elimination [8]. In addition, each type of TPS is characterised by a unique aspartate-rich motif; most type I TPSs have a DDXXD/E motif and an NSE/DTE motif, whereas type II TPSs have the DXDD motif [9][10

Inherent atomic mobility changes in carbocation intermediates during the sesterterpene cyclization cascade

• Hajime Sato,
• Takaaki Mitsuhashi,
• Mami Yamazaki,
• Ikuro Abe and
• Masanobu Uchiyama

Beilstein J. Org. Chem. 2019, 15, 1890–1897, doi:10.3762/bjoc.15.184

• intermediates, which reflect the initial conformation of the substrate, geranylfarnesyl diphosphate (GFPP). However, it remains unclear how the initial conformation of GFPP is controlled, and which part(s) of the GFPP molecule are important for its fixation inside the substrate-binding pocket. Here, we present

• terpene cyclase active site [3][5][6]. Although many terpene cyclases are known [6][7][8][9][10], it is still challenging to identify the precise initial conformation of the oligoprenyl diphosphate substrate in the active site, even by X-ray crystal structure determination. This is because the substrate

• diphosphate, IM: intermediate. Quiannulatene is formed by the deprotonation of IM11. Phase (I): 5/12/5 tricycle formation is highlighted in blue. Phase (II): conformational changes and hydrogen shifts are highlighted in orange. Phase (III): ring rearrangements are highlighted in yellow. Reaction mechanisms of

Molecular basis for the plasticity of aromatic prenyltransferases in hapalindole biosynthesis

• Takayoshi Awakawa and
• Ikuro Abe

Beilstein J. Org. Chem. 2019, 15, 1545–1551, doi:10.3762/bjoc.15.157

• ; prenyltransferase; Introduction Aromatic prenyltransferases (PTases) catalyze Friedel–Crafts reactions between aromatic prenyl acceptors and isoprenoid diphosphate prenyl donors to construct C–C, C–O, or C–N bonds, which enrich the structural diversity of aromatic natural products [1][2]. Their reactions are

• divided into two types, depending on where the cation is generated in the isoprenoid diphosphate: the “normal” prenylation in which the C-1 is attacked and the “reverse” prenylation in which the C-3 is attacked (Figure 1). It is important to study prenylation types for the chemoenzymatic synthesis of

• compounds, including dihydroxynaphthalenes, flavonoids, and resorcinols as prenyl acceptors, and C10 geranyl diphosphate (GPP) as a prenyl donor, to generate a variety of O- or C-prenylated aromatic compounds [4][10]. Some PTases accept multiple lengths of isoprenoid diphosphates, as exemplified by the ABBA

Phylogenomic analyses and distribution of terpene synthases among Streptomyces

• Lara Martín-Sánchez,
• Kumar Saurabh Singh,
• Mariana Avalos,
• Gilles P. van Wezel,
• Jeroen S. Dickschat and
• Paolina Garbeva

Beilstein J. Org. Chem. 2019, 15, 1181–1193, doi:10.3762/bjoc.15.115

• depends on the precursors that these synthases can accommodate: geranyl diphosphate (monoterpenes, C10), farnesyl diphosphate (sesquiterpenes, C15) and geranylgeranyl diphosphate (diterpenes, C20). The biological function of terpenes is best studied for plants where they play important roles in

Mechanistic investigations on multiproduct β-himachalene synthase from Cryptosporangium arvum

• Jan Rinkel and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2019, 15, 1008–1019, doi:10.3762/bjoc.15.99

• diphosphate. In-depth mechanistic investigations using isotopically labelled precursors regarding the stereochemical course of both 1,11-cyclisation and 1,3-hydride shift furnished a detailed catalytic model suggesting the molecular basis of the observed low product selectivity. The enzyme’s synthetic

• functional characterisation (Table S1, Supporting Information File 1). The purified recombinant protein (Figure S3, Supporting Information File 1) was incubated with the common TS substrates geranyl- (GPP, C10), farnesyl- (FPP, C15), geranylgeranyl- (GGPP, C20) and geranylfarnesyl (GFPP, C25) diphosphate

• . Whereas the latter diphosphate did not lead to any terpene product, the incubation with FPP showed a smooth conversion into several sesquiterpenes (Figure 1A) with compound 1 as the major peak after GC–MS analysis. However, also the incubations with GPP (Figure 1B) and GGPP (Figure 1C) led to several less

Stereochemical investigations on the biosynthesis of achiral (Z)-γ-bisabolene in Cryptosporangium arvum

• Jan Rinkel and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2019, 15, 789–794, doi:10.3762/bjoc.15.75

• sesquiterpene. Since the stereoinformation of both chiral putative intermediates, nerolidyl diphosphate (NPP) and the bisabolyl cation, is lost during formation of the achiral product, the intriguing question of their absolute configurations was addressed by incubating both enantiomers of NPP with the

• ; carbocation chemistry; enzyme mechanisms; nerolidyl diphosphate; terpenes; Introduction Given the enormous impact of chirality within biomolecules for all forms of life, it is fascinating to see how nature is able to maintain and reproduce stereochemical information. This concept largely involves the

• providing a defined cavity including its molecular coating together with binding and activation of the diphosphate (OPP) moiety, these enzymes convert simple achiral oligoprenyl diphosphates into often complex, polycyclic hydrocarbons or alcohols with introduction of multiple stereocentres in just one

Computational characterization of enzyme-bound thiamin diphosphate reveals a surprisingly stable tricyclic state: implications for catalysis

• Ferran Planas,
• Michael J. McLeish and
• Fahmi Himo

Beilstein J. Org. Chem. 2019, 15, 145–159, doi:10.3762/bjoc.15.15

• Abstract Thiamin diphosphate (ThDP)-dependent enzymes constitute a large class of enzymes that catalyze a diverse range of reactions. Many are involved in stereospecific carbon–carbon bond formation and, consequently, have found increasing interest and utility as chiral catalysts in various biocatalytic

• . Keywords: binding site; DFT; enzyme mechanism; quantum chemical calculations; ThDP-dependent; Introduction Enzymes that depend on thiamin diphosphate (ThDP, Scheme 1) can be found in a wide range of metabolic pathways. Although they are known to catalyze the formation of C–N, C–O and C–S bonds, ThDP

• has been observed on at least two ThDP-dependent enzymes. Dihydrothiachromine diphosphate (TC) was observed in the X-ray structure of phosphoketolase from Bifidobacterium breve [46], and its hydroxyethyl derivative was identified in the structure of acetolactate synthase from Klebsiella pneumoniae

Synthesis of new p-tert-butylcalix[4]arene-based polyammonium triazolyl amphiphiles and their binding with nucleoside phosphates

• Vladimir A. Burilov,
• Guzaliya A. Fatikhova,
• Mariya N. Dokuchaeva,
• Ramil I. Nugmanov,
• Diana A. Mironova,
• Pavel V. Dorovatovskii,
• Victor N. Khrustalev,
• Svetlana E. Solovieva and
• Igor S. Antipin

Beilstein J. Org. Chem. 2018, 14, 1980–1993, doi:10.3762/bjoc.14.173

• for nucleotides sensing through a dye replacement procedure. It is unusual that disubstituted macrocycles 10a,b bind more effectively a less charged adenosine 5'-diphosphate (ADP) than adenosine 5'-triphosphate (ATP). A simple colorimetric method based on polydiacetylene vesicles decorated with 10b

• are very important as a universal energy source and as intracellular mediators in many biological processes [6]. In the cellular metabolism, adenosine 5'-triphosphate (ATP) is hydrolyzed to adenosine 5'-monophosphate (AMP) or adenosine 5'-diphosphate (ADP) by enzymes [7]. Thus, the receptors for

• this reason the triphosphate fragment is rotated by ≈60° around the calixarene axis relative to the diphosphate position (Figure 4b and d). This leads to a weakening of the host–guest binding and to a decrease of ATP complex energy by 1.4 kcal/mol compared to ADP. So the ADP/ATP optical responses for

Mechanochemistry of nucleosides, nucleotides and related materials

• Olga Eguaogie,
• Joseph S. Vyle,
• Patrick F. Conlon,
• Manuela A. Gîlea and
• Yipei Liang

Beilstein J. Org. Chem. 2018, 14, 955–970, doi:10.3762/bjoc.14.81

• ) and adenosine diphosphate ribose (ADPR) was also described. Subsequently, this methodology was applied to the preparation of a library of six ADPR carbonate derivatives in 23–68% yields (e.g., Scheme 14) and tested as sirtuin inhibitors [54]. The efficiency of phosphate coupling under mechanochemical