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Adamantane

Q: What are the common applications of Adamantane?

Adamantane and its derivatives have been studied extensively and have a variety of applications. They are used in organic synthesis as building blocks, in materials science for their unique properties, and in medicinal chemistry for their potential pharmaceutical uses. Adamantane-based compounds have been investigated for their antimicrobial, antiviral, and other biological activities.

Q: How can PubCompare.ai help with Adamantane research?

PubCompare.ai allows you to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform can help researchers identify the most effective protocols related to Adamantane for their specific research goals. The AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibilty and accuracy in your Adamantane studies.

Q: Are there different variations or types of Adamantane?

Yes, there are several derivatives and analogs of Adamantane that have been synthesized and studied. These include substituted Adamantanes, Adamantane-containing heterocycles, and functionalized Adamantane compounds. The specific properties and applications of these Adamantane variations can vary depending on the substituents and modifications made to the core structure.

Q: What are some common challenges in using Adamantane?

One of the main challenges in working with Adamantane is its relatively low solubility in many solvents, which can make it difficult to incorporate into certain applications. Additionally, the rigid and bulky nature of the Adamantane structure can present steric hinderance in some chemical reactions and formulations. Researchers must carefully consider these factors when designing Adamantane-based compounds and processes to optimize their performance.

Adamantane is a cyclic, aliphatic hydrocarbon compound with the molecular formula C10H16.
It is a colorless, crystalline solid with a distinctive, camphor-like odor.
Adamantane and its derivatives have a wide range of applications in organic synthesis, materials science, and medicinal chemistry due to their unique chemical and physical properties.
This versatile compound has been studied extensively, with research focusing on its synthesis, reactivity, and potential uses in various fields.
PubCompare.ai can help optimize your Adamantane research by allowing you to easily locate and compare protocols from literature, preprints, and patents, enhacing reproducibility and accracy.
Experiencs the power of PubCompare.ai today to identify the best protocols and products for your Adamantane studies, streamlining your research process.

Most cited protocols related to «Adamantane»

Solid-State NMR Characterization of Water-Protein Interactions

Cited 13 times

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Publication 2014

Adamantane Crossing Over, Genetic Diffusion Phosphorylcholine

Guest-Host Hydrogel Characterization

Cited 7 times

For all characterization studies, hydrogels were prepared from stock solutions of the individual macromers in PBS at the desired concentration. For hydrogel formation by the guest-host assembly mechanism, the two component solutions were combined and mixed by manually stirring to ensure a homogenous hydrogel which was then briefly centrifuged to remove entrapped air. Unless otherwise stated, adamantane and β-cyclodextrin were present in stoichiometric balance, and the concentration refers to the overall weight percent of combined macromers.

Rodell C.B., Kaminski A, & Burdick J.A. (2013). Rational Design of Network Properties in Guest-Host Assembled and Shear-Thinning Hyaluronic Acid Hydrogels. Biomacromolecules, 14(11), 10.1021/bm401280z.

Publication 2013

Adamantane Cyclodextrins Homozygote Hydrogels

NMR Spectroscopy for Structural Analysis of Biomolecules

Cited 6 times

Histidine, glutamine, MLF, and M2TM spectra were measured on a Bruker 400 MHz spectrometer, while glucose and plant cell wall spectra were measured on a Bruker 600 MHz NMR spectrometer. Typical radiofrequency field strengths were ~70 kHz for ¹H decoupling and 50 kHz for ¹³C pulses. All ¹³C chemical shifts were externally referenced to the adamantane CH₂ peak at 38.48 ppm on the TMS scale.
The pulse sequence for the relaxation-compensated PDSD experiment (Fig. 1) contains a z-filter before the evolution period, and the sum of the z-filter (t_z) and mixing time (t_m) is kept constant to compensate for T₁ relaxation. Glutamine, histidine and MLF spectra were measured at room temperature using constant z-periods of 0.505 s, 1.005 s, and 1.505 s, respectively, and the MAS frequencies ranged from 7 to 10 kHz (Table S1). The M2TM spectra were measured with a constant z-period of 1.505 s at 273 K under 9 kHz MAS. The glucose and plant cell wall samples were measured using a constant z-period of 1.005 s under 8 kHz MAS. The temperature was 273 K for glucose and 253 K for the plant cell wall.
The difference spectra were obtained by subtracting a short mixing-time spectrum from a long mixing-time spectrum, with an adjustable scaling factor for the former. For the histidine difference spectrum, no scaling was applied. For glucose, the difference spectrum between 1.0 s and 0.2 s involved scaling the latter by 0.95 to give null intensities, while the difference spectrum between 200 ms and 20 ms involved scaling the 20 ms spectrum by 0.78 to remove the one-bond cross peaks. For MLF, a difference spectrum between 300 ms and 30 ms used a scaling factor of 0.35 to remove one-bond cross peaks. For influenza M2TM, a scaling factor of 0.70 was applied to the 100 ms spectrum before subtraction from the 1.5 s spectrum. For the plant cell wall sample, the relaxation-compensated difference between the 1.0 s and 0.2 s spectra used a scaling factor of 0.78 for the latter, while a regular PDSD difference spectrum used a scaling factor of 0.69 for the 0.2 s spectrum.

Wang T., Williams J.K., Schmidt-Rohr K, & Hong M. (2014). Relaxation-Compensated Difference Spin Diffusion NMR for Detecting 13C-13C Long-Range Correlations in Proteins and Polysaccharides. Journal of biomolecular NMR, 61(2), 97-107.

Publication 2014

A-factor (Streptomyces) A 300 Adamantane Biological Evolution factor A Glucose Glutamine Histidine Plant Cells Pulse Rate Pulses Virus Vaccine, Influenza

1D NMR Acquisition Parameters for Biomolecules

Cited 5 times

The 1D ¹⁵N-¹³C spectra were obtained at a spinning frequency of 13.0 kHz, on a custom-built spectrometer (courtesy of Dr. D. Ruben, Francis Bitter Magnet Laboratory/MIT, Cambridge, MA) operating at 750 MHz ¹H Larmor frequency and equipped with a triple-resonance ¹H/¹³C/¹⁵N 3.2 mm E-free probe (Bruker Biospin, Billerica MA).
The NCO SPECIFIC-CP condition was optimized to match 2.5 times the rotor frequency (ω_r) on ¹⁵N (~32.5 kHz) and 3.5 × ω_r on ¹³C (45.5 kHz), with 100 kHz ¹H CW decoupling during the transfer. The ¹³C carrier was set to the middle of the CO region (176 ppm), the ¹⁵N carrier to 115 ppm, and the ¹H carrier to 4 ppm.
The NCa SPECIFIC-CP condition was optimized to match 1.5 × ω_r on ¹⁵N and 2.5 × ω_r on ¹³C, with 100 kHz ¹H CW decoupling during the transfer. The ¹³C carrier was set to 57 ppm, the ¹⁵N carrier to 115 ppm, and the ¹H carrier to 4 ppm. The optimal NCa contact time was found to be 6 ms for both GB1 and GvpA.
Broadband DCP was optimized for overall (both NCa and NCO) transfer efficiencies. This caused suboptimal NCO and NCa transfers individually, but gave the overall highest simultaneous signal. To achieve this, the ¹³C carrier was set to 110 ppm, with radio frequency matching conditions of 2.5 × ω_r on ¹⁵N (~32.5 kHz) and 3.5 × ω_r on ¹³C (45.5 kHz), and 100 kHz ¹H CW decoupling during the transfer. The optimal DCP contact time was found to be 7 ms for both GB1 and GvpA.
The ZF-TEDOR experiments were performed using 50 kHz for both ¹³C and ¹⁵N. The mixing period was optimized to 1.28 ms for one bond ¹⁵N-¹³C transfer. (Jaroniec et al. 2002b (link)).
For all 1D comparisons, 83 kHz TPPM ¹H decoupling was used during acquisition (total phase difference,18°; TPPM pulse length 5.8 μs). Chemical shifts were referenced using the DSS scale (Morcombe and Zilm 2003 (link)), with adamantane (40.48 ppm for ¹³C) as a secondary standard. Relative NCO transfer efficiencies were determined by integrating the region from 170 ppm to 182 ppm (omitting the carboxyl peaks) for GB1 and GV, while relative NCa transfer efficiencies were determined by integrating the region from 50 ppm to 63 ppm for GV and 47 ppm to 63 ppm for GB1, assuring that only polarization from Ca carbons was used to evaluate transfer efficiencies.

Daviso E., Eddy M.T., Andreas L.B., Griffin R.G, & Herzfeld J. (2013). Efficient Resonance Assignment of Proteins in MAS NMR by Simultaneous Intra- and Inter-residue 3D Correlation Spectroscopy. Journal of biomolecular NMR, 55(3), 257-265.

Publication 2013

Adamantane Carbon MS 28 Pulse Rate Ruthenium Ben Vibration

TEDOR-DARR NMR Pulse Sequence for Biomolecular Structure

Cited 4 times

The TEDOR-DARR pulse sequence for these experiments is shown in Figure 1. In these experiments, the dwell time in the ω₁ dimension was synchronized to twice the rotor period (corresponding to bandwidth of ω_R/2), in order to fold the nitrogen spinning sidebands onto the centerband and to retain the heteronuclear dipolar recoupling during each TEDOR period. As a consequence, the resonances of the amino terminus of the backbone and the lysine sidechains are folded. The chemical shifts were referenced using the DSS scale (Morcombe and Zilm 2003 (link)), with adamantane (40.48 ppm for ¹³C) as a secondary standard. All the data were processed with the nmrPipe (Delaglio et al. 1995 (link)), and subsequently analyzed using Sparky (Goddard and Kneller).
The 3D experiments on GB1 were performed using a custom-built spectrometer (courtesy of Dr. D. Ruben, Francis Bitter Magnet Laboratory/MIT, Cambridge, MA) operating at 700 MHz ¹H Larmor frequency and equipped with a triple-resonance ¹H/¹³C/¹⁵N probe with a 3.2 mm MAS stator (¹H/¹³C/¹⁵N Varian-Chemagnetics Palo Alto, CA). The spinning frequency of 13.3 kHz, regulated to ± 5 Hz using a Bruker (Bruker Biospin, Billerica, MA) spinning frequency controller, was set to avoid overlap of rotational resonance of the carbonyl sidebands with the aromatic and aliphatic signals in the acquisition dimension (ω₃). The ¹³C and ¹⁵N π/2 pulses were 5 μs. TPPM decoupling was 71 kHz (total phase difference,18°; TPPM pulse length 6.8 μs) during gaps between REDOR pulses and 71 kHz (total phase difference 22°; TPPM pulse length 6.8 μs) during evolution and acquisition periods. Mixing periods were 1.2 ms for ZF-TEDOR, optimized for one-bond transfers, and 40 ms for DARR. The 3D data set was acquired using 60 × 210 × 1024 points and dwell times of 150.4, 30 and 16 μs for ω₁, ω₂ and ω₃ respectively. Each FID averaged four scans using a recycle delay of 2.3 s for a total experimental time of 5.5 days.
The 3D experiments on gas vesicles were performed using a Bruker spectrometer (Bruker Biospin, Billerica, MA) operating at 900 MHz ¹H Larmor frequency and equipped with a triple-resonance 3.2 mm ¹H/¹³C/¹⁵N e-free MAS probe (Bruker Biospin, Billerica, MA). The spinning frequency of 16.6 kHz, regulated to ± 2 Hz, was set to avoid overlap of the carbonyl sidebands with the aromatic and aliphatic signals in the acquisition dimension (ω₃). The ¹⁵N and ¹³C π/2 pulses were 7.1 μs and 3.5 μs, respectively. TPPM decoupling was 83 kHz (total phase difference 18°; TPPM pulse length 5.7 μs) during gaps between REDOR pulses, evolution and acquisition periods. Mixing periods were 1.4 ms for ZF-TEDOR and 40 ms for DARR. The 3D data set was acquired using 56 × 210 × 1536 points and dwell times of 120, 30 and 6 μs for ω₁, ω₂ and ω₃,, respectively. Each FID averaged four scans using a recycle delay of 2.3 s for a total experimental time of 5.2 days.

Publication 2013

Adamantane Biological Evolution Lysine MS 1-2 Nitrogen Pulse Rate Pulses Radionuclide Imaging Recycling Ruthenium Ben Vertebral Column Vibration

Most recents protocols related to «Adamantane»

Optimizing FAAH Inhibitor Potency

Not available on PMC !

Example 37

To improve inhibition potency relative to FAAH, various portions of the t-TUCB molecule were modified to identify potential FAAH pharmacophores. The 4-trifluoromethoxy group on t-TUCB was modified to the unsubstituted ring (A-3), 4-fluorophenyl (A-2) or 4-chlorophenyl (A-26). Potency on both sEH and FAAH increased as the size and hydrophobicity of the para position substituent increased, with 4-trifluoromethoxy being the most potent on both enzymes. Substituting the aromatic ring for a cyclohexane (A-3) or adamantane (A-4) resulted in a complete loss in activity against FAAH. Results are summarized in Table 1 below.

TABLE 1

Modification of the 4-trifluoromethoxy group of t-TUCB

[Figure (not displayed)]

Stereo-IC₅₀(nM)

R²—N(R³)—L¹—chemistryhsEHhFAAH

t-TUCB[Figure (not displayed)]
[Figure (not displayed)]
trans0.8140

A1-[Figure (not displayed)]
[Figure (not displayed)]
trans309,200

A-2[Figure (not displayed)]
[Figure (not displayed)]
trans184,600

A-26[Figure (not displayed)]
[Figure (not displayed)]
trans7380

A-3[Figure (not displayed)]
[Figure (not displayed)]
trans6>1,000

A-4[Figure (not displayed)]
[Figure (not displayed)]
trans3>10,000

A-10[Figure (not displayed)]
[Figure (not displayed)]
81,800

Next, the center portion of the molecule was modified to further investigate the specificity of t-TUCB on FAAH. Switching the cyclohexane linker to a cis conformation (A-5) resulted in a 20-fold loss of potency while removing the ring and replacing it with a butane chain (A-6) resulted in a completely inactive compound. While this suggests the compound must fit a relatively specific conformation in the active site to be active, we found the aromatic linker had essentially the same potency on FAAH (A-7). Although many potent urea-based FAAH inhibitors have a piperidine as the carbamoylating nitrogen, the modification to piperidine here reduced potency 13-fold. Results are summarized in Table 2 below.

TABLE 2

Modification of the central portion of t-TUCB

[Figure (not displayed)]

Stereo-IC₅₀(nM)

R²—N(R³)—L¹—chemistryhsEHhFAAH

t-TUCB[Figure (not displayed)]
[Figure (not displayed)]
trans0.8140

A-5[Figure (not displayed)]
[Figure (not displayed)]
cis22,800

A-6[Figure (not displayed)]
[Figure (not displayed)]
15>10,000

A-7[Figure (not displayed)]
[Figure (not displayed)]
7170

Since none of the modifications at this point improved potency towards FAAH, we focused on the benzoic acid portion of the molecule as shown in Table 3. To determine the importance of the terminal acid, the corresponding aldehyde (A-20) and alcohol (A-24) in addition to the amide (A-19) and nitrile (A-11) were tested. While the amide had slightly improved potency, the more reduced forms of the acid (A-20 and A-24) and amide (A-11) had substantially less activity on FAAH. Converting the benzoic acid to a phenol (A-21) increased potency while the anisole (A-22) was completely inactive. Since the amide and acid appeared to be active, the amide bioisostere oxadiazole (A-25) was tested and had 38-fold less potency than the initial compound.

TABLE 3

Modification of the benzoic acid portion of t-TUCB

[Figure (not displayed)]

IC₅₀(nM)

R¹hsEHhFAAH

t-TUCB[Figure (not displayed)]
0.8140

A-11[Figure (not displayed)]
5>10,000

A-19[Figure (not displayed)]
270

A-20[Figure (not displayed)]
41,100

A-24[Figure (not displayed)]
35,800

A-21[Figure (not displayed)]
2120

A-22[Figure (not displayed)]
3>10,000

A-25[Figure (not displayed)]
45,300

Since the substrates for FAAH tend to be relatively hydrophobic lipids, we speculated that conversion of the acid and primary amide to the corresponding esters or substituted amides would result in improved potency. The methyl ester (A-12) had 4-fold improved potency relative to the acid. Improving the bulk of the ester with an isopropyl group (A-13) results in a 11-fold loss in potency relative to the methyl ester. However, the similar potency of the benzyl ester (A-14) to the methyl ester demonstrates the bulk but not the size affects potency. Reversing the orientation of the ester (A-23) reduces the potency 3.4-fold. Relative to the primary amide, the methyl (A-18), ethanol (A-15) and glycyl (A-16) amides were all slightly less potent; however, the benzyl amide (A-27) was substantially less potent (16-fold). Generating the methyl ester of the glycyl amide (A-17) increased the potency 4-fold compared to the corresponding acid.

TABLE 4

Potency of ester and amide conjugates of t-TUCB

[Figure (not displayed)]

IC₅₀(nM)

R¹hsEHhFAAH

t-TUCB[Figure (not displayed)]
0.8140

A-12[Figure (not displayed)]
735

A-13[Figure (not displayed)]
5400

A-14[Figure (not displayed)]
324

A-23[Figure (not displayed)]
4120

A-18[Figure (not displayed)]
2170

A-15[Figure (not displayed)]
2100

A-16[Figure (not displayed)]
2130

A-17[Figure (not displayed)]
330

A-27[Figure (not displayed)]
51,100

US11873288B2. Inhibitors for soluble epoxide hydrolase (sEH) and fatty acid amide hydrolase (FAAH) (2024-01-16). The Regents of the University of California [US]. Inventors: Bruce Hammock [US], Sean Kodani [US].

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Patent 2024

Acids Adamantane Aldehydes Amides anisole Benzoic Acid Butanes Cyclohexane Dietary Fiber Enzymes Esters Ethanol inhibitors Lipids Nitriles Nitrogen Oxadiazoles Phenol piperidine Psychological Inhibition SOCS2 protein, human Urea

Targeted Peptide-Nanoparticle Coupling

Not available on PMC !

Example 20

Coupling of the ligand to the nanoparticle may be achieved uniquely by following an inclusion compound protocol with β-cyclodextrin (β-CD) on the particle spontaneously interacting with adamantane on the peptide or small molecule ligand to form an inclusion complex. Briefly, cyclodextrin-PEG-DSPE derivative will be synthesized via mono-6-deoxy-6-amino-β-cyclodextrin. One of the seven primary hydroxyl groups of β-cyclodextrin will be tosylated using p-toluenesulfonyl chloride. Substitution of the tosyl group by azide and subsequent reduction with triphenylphosphine will yield mono-6-deoxy-6-amino-β-cyclodextrin. Carboxyl-activated PEG-DSPE will be conjugated to mono-6-deoxy-6-amino-β-cyclodextrin to produce cyclodextrin-PEG-DSPE. Adamantane-amine will be directly conjugated through a short spacer in the solid phase peptide synthesis to the carboxyl end of the peptide to produce adamantane-peptide/ligand. The simple room temperature mixing of adamantane-amine and β-cyclodextrin bearing nanoparticle will produce peptide coupled targeted nanoparticle.

US11872313B2. Prodrug compositions, prodrug nanoparticles, and methods of use thereof (2024-01-16). Washington University [US]. Inventors: Gregory M. Lanza [US], Dipanjan Pan [US].

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Patent 2024

4-toluenesulfonyl chloride Adamantane Amines Azides Cyclodextrins Hydroxyl Radical Ligands oxytocin, 1-desamino-(O-Et-Tyr)(2)- Peptides polyethylene glycol-distearoylphosphatidylethanolamine triphenylphosphine

NMR Data Processing Techniques

All MAS NMR data were processed using Bruker TopSpin and NMRpipe^{36 (link)}. The ¹³C and ¹⁵N signals were referenced with respect to the external standards adamantane and ammonium chloride, respectively. ¹H was referenced to the water peak at 4.7 ppm. ³¹P was referenced with respect to the phosphorous resonance of 85% H₃PO₄. The 2D and 3D data sets were processed by applying 30°, 45°, 60° and 90° shifted sine bell apodization followed by a Lorentzian-to-Gaussian transformation in both dimensions. Forward linear prediction to twice the number of the original data points was used in the indirect dimension in some data sets, followed by zero filling. The 2D CH HETCOR and dREDOR-HETCOR data of U-¹³C,¹⁵N,²H-CA_CTD-SP1 samples were processed with gaussian apodization and quadrature baseline correction.

Sarkar S., Zadrozny K.K., Zadorozhnyi R., Russell R.W., Quinn C.M., Kleinpeter A., Ablan S., Meshkin H., Perilla J.R., Freed E.O., Ganser-Pornillos B.K., Pornillos O., Gronenborn A.M, & Polenova T. (2023). Structural basis of HIV-1 maturation inhibitor binding and activity. Nature Communications, 14, 1237.

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Publication 2023

Adamantane Carnitine-Acylcarnitine Translocase Deficiency Chloride, Ammonium Phosphorus Short Interspersed Nucleotide Elements Vibration

Solid-State NMR Experimental Parameters

Magic-angle spinning (MAS) SSNMR experiments were performed at magnetic field of 11.7 T (500 MHz ¹H frequency) or 17.6 T (750 MHz ¹H frequency) using Agilent Technologies VNMRS spectrometers. Spinning was controlled with a Varian MAS controller to 11,111 ± 30 Hz or 22,222 ± 15 Hz (11.7 T) and 16,667 ± 15 Hz or 33,333 ± 30 Hz (17.6 T), with two minor exceptions indicated in Table 1. All experiments were done with a variable-temperature (VT) airflow setting of 0 °C, primarily to keep samples cool from RF and MAS heating, without freezing out molecular motions. The 11.7 T magnet was equipped with a 1.6 mm HCDN T3 probe (Varian), with pulse widths of about 1.8 μs for ¹H and ¹³C, and 3.2 μs for ¹⁵N. The 17.6 T magnet was equipped with a HXYZ T3 probe (Varian) tuned to HCN triple resonance mode with pulse widths of about 1.9 μs for ¹H, 2.6 μs for¹³C, and 3.0 μs for ¹⁵N. All experiments utilized ¹H-¹³C or ¹H-¹⁵N tangent ramped CP (Metz et al. 1994 ) and ~100 kHz SPINAL-64 decoupling during evolution and acquisition periods (Comellas et al. 2011, Fung et al. 2000 (link)). Where applicable, SPECIFIC CP was used for ¹⁵N-¹³Cα and ¹⁵N-¹³C’ transfers (Baldus et al. 1998 ), ¹³C-¹³C homonuclear mixing was performed using DARR (Takegoshi et al. 2001 ). Chemical shifts were externally referenced to the downfield peak of adamantane at 40.48 ppm (Morcombe and Zilm 2003 (link)). NUS schedules using biased exponential sampling were prepared using the nus-tool application in NMRbox (Maciejewski et al. 2017 (link)). Data conversion and processing was done with NMRPipe (Delaglio et al. 1995 (link)). NUS data was first expanded with the nusExpand.tcl script in NMRPipe, converted, and processed using the built-in SMILE reconstruction function (Ying et al. 2017 (link)). Peak picking and chemical shift assignments were performed using NMRFAM-Sparky (Lee et al. 2015 (link)).

Barclay A.M., Dhavale D.D., Borcik C.G., Milchberg M.H., Kotzbauer P.T, & Rienstra C.M. (2023). 13C and 15N Resonance Assignments of Alpha Synuclein Fibrils Amplified from Lewy Body Dementia Tissue. Research Square.

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Publication Preprint 2023

Adamantane Biological Evolution Magnetic Fields Pulse Rate Reconstructive Surgical Procedures Vibration

Comprehensive Nanomaterial Characterization Protocol

For the characterization of the nanomaterials, transmission electronic microscopy (TEM) measurements were carried out on a TECNAI G2 20 TWIN operated at 200 kV and equipped with LaB6 filament and high angle annular dark-field-scanning transmission electron microscopy (HAADF-STEM). TEM samples were prepared using a dispersion in ethanol applying ultrasounds for 15 min and adding a drop of the suspension to a TEM copper grid (300 Mesh) covered by a holey carbon film and drying the grid at room temperature. The micrographs were analyzed with ImageJ^©. Textural properties of samples were obtained by N₂ physisorption in Micromeritics ASAP 2020. Samples were degassed at 180 °C applying vacuum of 10 μm Hg during 8 h. The materials were then measured at −196 °C. Brunauer Emmett Teller (BET) and Barrett–Joyner–Halenda (BJH) studies of the desorption branch were used to determine the surface area and the pore size distribution. Inductively coupled plasma mass spectrometry (ICP-MS) measurements were recorded using an Agilent 7700 spectrometer, while a thermogravimetric analysis (TG) was carried out using a TG-Q500 TA Instrument thermal analyzer from 20 to 750 °C with a heating rate of 10 °C min⁻¹ and using a nitrogen atmosphere. The powder X-ray diffraction (XRD) patterns were collected on a Phillips X’PERT powder diffractometer with CuKα radiation (λ = 1.5418 Å) in the following ranges: 0.8 < 2θ < 10°, and with a step size of 0.026° with an acquisition time of 2.5 s per step at 25 °C. Fourier Transformed-infrared (IR) spectra (400–4000 cm⁻¹) were recorded on a Nicolet FT-IR 6700 spectrometer using KBr pellets. DR-UV measurements were carried out using a UV/Vis Shimadzu spectrophotometer. The spectra were obtained at room temperature using BaSO₄ as the reference material. ¹³C CP MAS NMR Solid-State nuclear magnetic resonance (NMR) measurements were carried out in a high-resolution mode, at 298 K on a Bruker Avance 400 WB spectrometer at 9.4 T, using 400.17 (¹H) and 100.66 MHz (¹³C) resonance frequencies. The ¹³C NMR experiments were recorded using a cross-polarization (CP) technique, high power decoupling, and magic angle spinning (MAS) with rates of 10 kHz, using a Bruker double-bearing probe head and 4 mm zirconia rotors driven by dry air. The Hartmann–Hahn conditions for ¹³C NMR were matched using adamantane. The recycle delay was 5 s and the contact time was 2 ms. Chemical shifts were determined by using an external standard based on glycine (Gly) (dCO of Gly= 176.5 ppm). Photoluminescence (PL) measurements were recorded at room temperature with a Varian Cary-Eclipse fluorescence spectrofluorometer with a Xe discharge lamp (peak power equivalent to 75 kW), Czerny–Turner monochromators, and an R-928 photomultiplier tube. The measurements were carried out at a photomultiplier detector voltage of 600 V, and with both the excitation and emission slits set at 5 nm.

Ugalde-Arbizu M., Aguilera-Correa J.J., García-Almodóvar V., Ovejero-Paredes K., Díaz-García D., Esteban J., Páez P.L., Prashar S., San Sebastian E., Filice M, & Gómez-Ruiz S. (2023). Dual Anticancer and Antibacterial Properties of Silica-Based Theranostic Nanomaterials Functionalized with Coumarin343, Folic Acid and a Cytotoxic Organotin(IV) Metallodrug. Pharmaceutics, 15(2), 560.

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Publication 2023

Adamantane Atmosphere Carbon Copper Cytoskeletal Filaments Ethanol Fever Fluorescence Glycine Head Magnetic Resonance Magnetic Resonance Imaging Mass Spectrometry Nitrogen Patient Discharge Pellets, Drug Plasma Powder Radiation Recycling Scanning Transmission Electron Microscopy TG-1101 Transmission Electron Microscopy Twins Ultrasonography Vacuum Vibration X-Ray Diffraction zirconium oxide

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Adamantane by Merck Group

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Adamantane is a colorless, crystalline hydrocarbon compound with the chemical formula C10H16. It is a rigid, cage-like molecule composed of four fused cyclohexane rings. Adamantane is known for its unique chemical structure and physical properties.

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What is Adamantane?

What are the common applications of Adamantane?

Adamantane and its derivatives have been studied extensively and have a variety of applications. They are used in organic synthesis as building blocks, in materials science for their unique properties, and in medicinal chemistry for their potential pharmaceutical uses. Adamantane-based compounds have been investigated for their antimicrobial, antiviral, and other biological activities.

How can PubCompare.ai help with Adamantane research?

PubCompare.ai allows you to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform can help researchers identify the most effective protocols related to Adamantane for their specific research goals. The AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibilty and accuracy in your Adamantane studies.

Are there different variations or types of Adamantane?

Yes, there are several derivatives and analogs of Adamantane that have been synthesized and studied. These include substituted Adamantanes, Adamantane-containing heterocycles, and functionalized Adamantane compounds. The specific properties and applications of these Adamantane variations can vary depending on the substituents and modifications made to the core structure.

What are some common challenges in using Adamantane?

One of the main challenges in working with Adamantane is its relatively low solubility in many solvents, which can make it difficult to incorporate into certain applications. Additionally, the rigid and bulky nature of the Adamantane structure can present steric hinderance in some chemical reactions and formulations. Researchers must carefully consider these factors when designing Adamantane-based compounds and processes to optimize their performance.

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