Amx 300

Dry solvents were purchased and stored under nitrogen over molecular sieves (bottles with crown caps). Reactions were monitored by analytical thin-layer chromatography (TLC) using silica gel 60 F 254 pre-coated glass plates (0.25 mm thickness) and visualized using UV light. Flash chromatography was carried out on silica gel (230–400 mesh). Proton NMR spectra were recorded on spectrometers operating at 300 MHz (Bruker Fourier 300 or AMX 300, Milano, Italy). Proton chemical shifts are reported in ppm (δ) with the solvent reference relative to tetramethylsilane (TMS) employed as the internal standard (CDCl₃ δ = 7.26 ppm). Commercial grade reagents and solvents were used without further purifications. Commercially available HSiCl₃was freshly distilled under nitrogen atmosphere before use. Reagents mixtures were fed to continuous flow reactors using Syringe Pump Chemix Fusion 100. Continuous flow catalytic reactors were prepared using Glass Omnifit columns (Sigma-Aldrich, Milano, Italy) equipped with one adjustable-length end piece.

All starting reagents/chemicals and dry solvents of commercial quality were purchased from the commercial suppliers VWR Darmstadt/Germany, Acros, Geel/Belgium, Alfar Aesar, Ward Hill/U.S.A., Sigma-Aldrich, St. Louis/USA, Fluka, München/Germany and Carl Roth, Karlsruhe/Germany. ¹H-NMR and ¹³C-NMR spectra were recorded on a Bruker AMX 250 (250 MHz), a Bruker AMX 300 (300 MHz) or a Bruker AMX 400 (400 MHz) spectrometer (Bruker, Germany). ¹H-NMR data are reported in the following order: chemical shift (δ) in ppm downfield from tetramethylsilane as internal reference; multiplicity (br, broad; s, singlet; d, doublet; t, triplet; q, quartet; quin, quintet; m, multiplet); approximate coupling constants (J) in Hertz (Hz). ESI-MS was performed on a Fisons Instruments VG Platform II (Manchester, Great Britain) in positive polarity. Data (m/z) are listed as mass number (M+H⁺) and relative intensity (%). MALDI_MS was performed on Voyager DE STR (Per Septive Biosystems). High Resolution Mass Spectrometry (HRMS) was carried out on a Thermo Scientific MALDI LTQ XL Orbitrap (Waltham, USA). Thin layer chromatography was performed on silica gel 60 F₂₅₄ aluminum sheets (Merck, Germany). Preparative column chromatography was performed on silica gel 63–200 μM (Merck, Germany). Melting points were determined on a Büchi B510 melting point apparatus (Büchi, Switzerland).

Starting materials were either commercially available or synthesized according to methods reported in the literature. ¹H and ¹³C NMR spectra were recorded on either a Bruker AMX-300 or a Bruker AMX-500 spectrometer. Chemical shifts are reported as ppm relative to TMS internal standard. Mass spectra were recorded on either a Fisons VG70-SE spectrometer (EI, FAB) or an Agilent 6100 Series LC-mass spectrometer (Wokingham, Berkshire, UK) using either a C-18 or C-4 column. Microwave reactions were carried out using a CEM Discover microwave. All compounds were purified to ≥ 95% as measured by LC-MS. Proteoglycan binding was recorded using an Agilent 1200 series HPLC system equipped with a diode array detector and HiTrap heparin agarose column. A complete list of ¹H NMRs for compounds used in this study is given in the supplementary information (Table S1).

Monodimensional ¹⁹⁵Pt-NMR, ¹³C-NMR and ¹H-NMR experiments were performed in DMSO-d₆ and D₂O using a Bruker AMX-300 (300 MHz) spectrometer at room temperature (25°C). Elemental analyses were performed with a PerkinElmer 2400 Series II microanalyzer. IR was performed with a PerkinElmer Model 283 spectrophotometer with an ATR accessory (Miracle Single Reflection Horizontal). UV–visible spectroscopy was performed with a Thermo Fisher Scientific Evolution 260 Bio spectrophotometer. Mass spectrometry was performed with a QSTAR de ABSciex by electrospray.

Unless otherwise stated, all
reactions and manipulations were carried out under an atmosphere of
dry argon or nitrogen using standard Schlenk techniques or in a nitrogen
glovebox. Solvents were distilled under an inert atmosphere prior
to use. Solution ¹H, ¹³C, and ³¹P
NMR spectra were recorded on Bruker AMX-300, DRX-400, and DRX-500
spectrometers at 298 K unless otherwise stated. Chemical shifts (δ)
are expressed with a positive sign, in parts per million. ¹H and ¹³C chemical shifts reported are referenced internally
to residual protio (¹H) or deutero (¹³C) solvent,
while ³¹P chemical shifts are relative to 85% H₃PO₄. The following abbreviations and their combinations
are used: br, broad; s, singlet; d, doublet; t, triplet; m, multiplet.
The ¹H and ¹³C resonance signals were attributed
by means of two-dimensional (2D) HSQC and HMBC experiments (Figure 5). Infrared spectra
were recorded with a Bruker Vector 22 spectrometer, and sample preparation
was carried out in dichloromethane solution. For elemental analyses,
a LECO TruSpec CHN elementary analyzer was utilized. Complex 1 was prepared according to a literature procedure.^{13 (link)} All other reagents were used as received from
commercial suppliers. The yields obtained for complexes 3, 4, 7, 8, and 12 have been calculated taking into account the amount of residual
pentane observed by ¹H and ¹³C NMR spectroscopy
in the samples.

Four independent photoisomerization experiments were performed using different initial concentrations of azoCyDdimer: 15 mM, 8 mM, 2.28 mM, and 0.5 mM. Dilutions were made from a 15 mM stock solution with an isomer ratio of 95:5 (E:Z). The stock solution and the dilutions were irradiated at 360 nm for 20 min, and then the corresponding ¹HRMN spectra were acquired (AMX 300, Bruker, Germany), protecting the solution from the visible light. Switching experiments were performed with an 8 W mercury arc lamp with filter of 360 nm from Pleuger, Antwerp, Brussels.