Development of a chemical scaffold for inhibiting nonribosomal peptide synthetases in live bacterial cells

• Fumihiro Ishikawa,
• Sho Konno,
• Hideaki Kakeya and
• Genzoh Tanabe

Beilstein J. Org. Chem. 2024, 20, 445–451, doi:10.3762/bjoc.20.39

• , Supporting Information File 1). After washing, the wells were incubated with an anti-His6 tag antibody and subsequently with a horseradish peroxidase-conjugated secondary antibody. The amount of GrsA bound to ʟ-Phe-AMS-biotin was determined by measuring the absorbance of o-phenylenediamine dihydrochloride at

Non-peptide compounds from Kronopolites svenhedini (Verhoeff) and their antitumor and iNOS inhibitory activities

• Yuan-Nan Yuan,
• Jin-Qiang Li,
• Hong-Bin Fang,
• Shao-Jun Xing,
• Yong-Ming Yan and
• Yong-Xian Cheng

Beilstein J. Org. Chem. 2023, 19, 789–799, doi:10.3762/bjoc.19.59

• separated by 10% SDS-PAGE and transferred onto PVDF membranes. The membranes were blocked with 5% BSA and incubated with the indicated antibodies overnight at 4 °C. Following this, the membranes were incubated with horseradish peroxidase (HRP)-conjugated secondary antibody at room temperature. The ECL kit

Chemical approaches to discover the full potential of peptide nucleic acids in biomedical applications

• Nikita Brodyagin,
• Martins Katkevics,
• Venubabu Kotikam,
• Christopher A. Ryan and
• Eriks Rozners

Beilstein J. Org. Chem. 2021, 17, 1641–1688, doi:10.3762/bjoc.17.116

Oxime radicals: generation, properties and application in organic synthesis

• Igor B. Krylov,
• Stanislav A. Paveliev,
• Alexander S. Budnikov and
• Alexander O. Terent’ev

Beilstein J. Org. Chem. 2020, 16, 1234–1276, doi:10.3762/bjoc.16.107

• [46], Pb(OAc)4 [44][46][47][48][49][50][51], PbO2 [52], Mn(OAc)3 [46], KMnO4 [46], Ag2O [53], AgO [54], Horseradish peroxidase/H2O2 [55], metal-free oxidants PhI(OAc)2 [46], t-BuOOt-Bu [53] or quinones [56] under UV irradiation. Anodic oxidation was also reported [57]. The establishing of the self

Towards the preparation of synthetic outer membrane vesicle models with micromolar affinity to wheat germ agglutinin using a dialkyl thioglycoside

• Dimitri Fayolle,
• Nathalie Berthet,
• Bastien Doumeche,
• Olivier Renaudet,
• Peter Strazewski and
• Michele Fiore

Beilstein J. Org. Chem. 2019, 15, 937–946, doi:10.3762/bjoc.15.90

• horseradish peroxidase-labelled (WGA-HRP) to a GlcNAc-polyacrylamide conjugate following the procedure described in Figure 4. WGA is a homodimer in which each monomer is organized into four domains (A–D) containing adjacent “primary” (B and C) and “secondary” (A and D) domains binding sites with different

• Lipids (Alabaster, AL, USA). 2,3,4,6-Tetra-O-acetyl-α--glucopyranosyl bromide and N-acetyl--glucosamine were from Carbosynth (San Diego, CA, USA). Wheat germ agglutinin (WGA), horseradish peroxidase-labelled WGA (WGA-HRP), bovine serum albumin (BSA) and SIGMA FAST O-phenylenediamine dihydrochloride (OPD

Biocatalytic synthesis of the Green Note trans-2-hexenal in a continuous-flow microreactor

• Morten M. C. H. van Schie,
• Tiago Pedroso de Almeida,
• Gabriele Laudadio,
• Florian Tieves,
• Elena Fernández-Fueyo,
• Timothy Noël,
• Isabel W. C. E. Arends and
• Frank Hollmann

Beilstein J. Org. Chem. 2018, 14, 697–703, doi:10.3762/bjoc.14.58

• spectrophotometer, following the oxidation of ABTS (ε405 = 36,800 M−1 cm−1) by horseradish peroxidase (POD) at the expense of hydrogen peroxide. In general, 0.044 µM PeAAOx was used to convert 3 mM of trans-2-hex-2-enol. The hydrogen peroxide formed in this reaction was subsequently used to convert 2 mM of ABTS to

• -catalysed oxidation of trans-hex-2-enol. Conditions: 50 mM KPi buffer (pH 7, 30 °C), [trans-hex-2-enol]0 = 3 mM, [PeAAOx] = 0.044 µM, [horseradish peroxidase] = 500 U mL−1, [ABTS] = 2 mM. The influence of the residence time on the conversion of trans-hex-2-enol (red squares) to trans-2-hexenal (black

Carbohydrate inhibitors of cholera toxin

• Vajinder Kumar and
• W. Bruce Turnbull

Beilstein J. Org. Chem. 2018, 14, 484–498, doi:10.3762/bjoc.14.34

• lower that for the tetravalent compound 22b (IC50 = 160 ± 40 pM) [56]. Inhibition results described in this review are essentially all derived from very similar types of enzyme-linked lectin assays (ELLA) in which the inhibitors are used to prevent CTB-linked horseradish peroxidase from binding to

Expression, purification and structural analysis of functional GABA transporter 1 using the baculovirus expression system

• Jing Hu,
• Chris Weise,
• Christoph Böttcher,
• Hua Fan and
• Jian Yin

Beilstein J. Org. Chem. 2017, 13, 874–882, doi:10.3762/bjoc.13.88

• polyclonal antiserum. Subsequently, the blots were incubated with horseradish peroxidase-conjugated anti-rabbit antibody (IgG) (Dako Cytomation) and then visualized using amino ethylcarbazole (AEC) and substrate buffer (Calbiochem). Flow cytometry and fluorescence microscopy Sf9 cells were observed after 3

Unconventional application of the Mitsunobu reaction: Selective flavonolignan dehydration yielding hydnocarpins

• Guozheng Huang,
• Simon Schramm,
• Jörg Heilmann,
• David Biedermann,
• Vladimír Křen and
• Michael Decker

Beilstein J. Org. Chem. 2016, 12, 662–669, doi:10.3762/bjoc.12.66

• ; 5% catalyzed by horseradish peroxidase) [14]. To study the biological activities of hydnocarpin-type compounds, a new and robust method for their preparation is required. It is known that elimination can occur in some cases as a side reaction in Mitsunobu esterifications with structurally hindered

Oligomerization of optically active N-(4-hydroxyphenyl)mandelamide in the presence of β-cyclodextrin and the minor role of chirality

• Helmut Ritter,
• Antonia Stöhr and
• Philippe Favresse

Beilstein J. Org. Chem. 2014, 10, 2361–2366, doi:10.3762/bjoc.10.246

• .10.246 Abstract The oxidative oligomerization of a chiral mandelamide derivative (N-(4-hydroxyphenyl)mandelamide, 1) was performed in the presence of horseradish peroxidase, laccase and N,N'-bis(salicylidene)ethylenediamine-iron(II) to obtain chiral oligophenols 2. The low enantioselectivity of the

• converted with both enzymes. However this preference is very low in all cases. Experimental Materials Horseradish peroxidase practical grade I (370,2 U/mg) was purchased from Appli Chem and Laccase from pleurotus ostreatus (9,4 U/mg) from Sigma-Aldrich. p-Aminophenol was bought from Grüssing, N,N

Expanding the scope of cyclopropene reporters for the detection of metabolically engineered glycoproteins by Diels–Alder reactions

• Anne-Katrin Späte,
• Verena F. Schart,
• Julia Häfner,
• Andrea Niederwieser,
• Thomas U. Mayer and
• Valentin Wittmann

Beilstein J. Org. Chem. 2014, 10, 2235–2242, doi:10.3762/bjoc.10.232

• antibody (AA4.3, hypridoma supernatant in 1% FCS, 1:200 dilution in milk) for 1 h at rt. The membranes were washed (3 times, 10–15 min, PBS-T), incubated with secondary horseradish-peroxidase-conjugated anti-mouse antibody (Dianova, goat anti-mouse IgG (H+L)-HRP, 1:50000 dilution in milk, 1 h, rt), and

Physalin H from Solanum nigrum as an Hh signaling inhibitor blocks GLI1–DNA-complex formation

• Midori A. Arai,
• Kyoko Uchida,
• Samir K. Sadhu,
• Firoj Ahmed and
• Masami Ishibashi

Beilstein J. Org. Chem. 2014, 10, 134–140, doi:10.3762/bjoc.10.10

• –515 amino chain, including the five Zn finger regions. Horseradish peroxidase (HRP)-conjugated streptavidin detected free “biotin-labeled GLI1-BS” (DNA containing GLI1 binding site; biotin-AGCTACCTGGGTGGTCTCTTCGA; the underlined 9 bps are a consensus sequence [30]; Figure 5, lane 1). After mixing with

New enzymatically polymerized copolymers from 4-tert-butylphenol and 4-ferrocenylphenol and their modification and inclusion complexes with β-cyclodextrin

• Adam Mondrzyk,
• Beate Mondrzik,
• Sabrina Gingter and
• Helmut Ritter

Beilstein J. Org. Chem. 2012, 8, 2118–2123, doi:10.3762/bjoc.8.238

• (N3-β-CD) was carried out. The formation of inter- and intramolecular inclusion complexes was investigated by DLS measurement. Keywords: copolymer; ß-cyclodextrin; enzymatic polymerization; 4-ferrocenylphenol; polyphenol; 4-tert-butylphenol; horseradish peroxidase; HRP oxidative coupling; inclusion

High-affinity multivalent wheat germ agglutinin ligands by one-pot click reaction

• Henning S. G. Beckmann,
• Heiko M. Möller and
• Valentin Wittmann

Beilstein J. Org. Chem. 2012, 8, 819–826, doi:10.3762/bjoc.8.91

• ’-diacetylchitobiose were determined by an ELLA employing covalently immobilized GlcNAc as a reference ligand, as described recently [34]. GlcNAc-coated microtiter plates were incubated with mixtures of horseradish-peroxidase-labeled WGA (HRP-WGA) and synthetic WGA ligands in varying concentrations. After incubation

An easily accessible sulfated saccharide mimetic inhibits in vitro human tumor cell adhesion and angiogenesis of vascular endothelial cells

• Grazia Marano,
• Claas Gronewold,
• Martin Frank,
• Anette Merling,
• Christian Kliem,
• Sandra Sauer,
• Manfred Wiessler,
• Eva Frei and
• Reinhard Schwartz-Albiez

Beilstein J. Org. Chem. 2012, 8, 787–803, doi:10.3762/bjoc.8.89

Miniemulsion polymerization as a versatile tool for the synthesis of functionalized polymers

• Daniel Crespy and
• Katharina Landfester

Beilstein J. Org. Chem. 2010, 6, 1132–1148, doi:10.3762/bjoc.6.130

• solution polymerization was demonstrated by Qi et al. who were able to polymerize styrene with horseradish peroxidase, hydrogen peroxide, and a β-diketone in aqueous direct miniemulsion [92]. Normally, only hydrophilic monomers can be polymerized with this initiating system in water or a co-solvent, e.g