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(1S)-(-)-Camphor Sale

(Synonyms: 左旋樟脑) 目录号 : GC40695

A monoterpene with acaricidal activity

(1S)-(-)-Camphor Chemical Structure

Cas No.:464-48-2

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100mg
¥1,542.00
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产品描述

(1S)-(-)-Camphor is a monoterpene found in various plant extracts, including P. suffructicosa with acaricidal activity. It exhibits fumigant toxicity against T. putrescentiae when used at a concentration of 10.45 mg.

Chemical Properties

Cas No. 464-48-2 SDF
别名 左旋樟脑
Canonical SMILES O=C1C[C@@H]2CC[C@]1(C2(C)C)C
分子式 C10H16O 分子量 152.2
溶解度 DMF: 30 mg/ml,DMSO: 20 mg/ml,Ethanol: 30 mg/ml,Ethanol:PBS (pH 7.2)(1:2): 0.33 mg/ml 储存条件 Store at -20°C
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1 mM 6.5703 mL 32.8515 mL 65.703 mL
5 mM 1.3141 mL 6.5703 mL 13.1406 mL
10 mM 0.657 mL 3.2852 mL 6.5703 mL
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Research Update

Fragmentation dynamics of doubly charged camphor molecule following C 1S Auger decay

Phys Chem Chem Phys 2022 Feb 2;24(5):2944-2957.PMID:35076648DOI:10.1039/d1cp05176h.

The fragmentation dynamics of the gas-phase, doubly charged camphor molecule, formed by Auger decay following carbon 1S ionisation, using soft X-ray synchrotron radiation, is presented in this work. The technique of velocity map imaging combined with a photoelectron-photoion-photoion coincidence (VMI-PEPIPICO) is used for both electron energy and ion momentum (in-sequence) measurements. The experimental study is complemented by molecular dynamics simulation, performed with an NVT (moles, volume, and temperature) ensemble. Velocity Verlet algorithms were used for time integration at various internal energies. These simulations validate observed dissociation pathways. From these, we successfully deduce that the internal energy of the doubly charged molecular ion has a significant contribution to the fragmentation mechanism. Notably, a prominent signature of the internal energy was observed in the experimentally determined energies of the neutral fragment in these deferred charge separation pathways, entailing a more detailed theoretical study to uncover the exact dissociation dynamics.

Ammonium [(1S)-(endo,anti)]-(-)-3-bromo-camphor-8-sulfonate

Acta Crystallogr Sect E Struct Rep Online 2010 Jun 18;66(Pt 7):o1707-8.PMID:21587927DOI:10.1107/S1600536810022804.

In the title mol-ecular salt, NH(4) (+)·C(10)H(14)BrO(4)S(-), the norbornane skeleton of the anion is composed of two five-membered rings in envelope conformations and a six-membered ring with one Br atom, one carbonyl O atom and a methyl group held in a boat conformation by a bridging methyl-ene group. Short intra-molecular C-H⋯O and C-H⋯Br inter-actions occur. In the crystal, the component ions are linked by inter-molecular N-H⋯O and C-H⋯O hydrogen bonds.

Detecting stable adsorbates of (1 S)-camphor on Cu(111) with Bayesian optimization

Beilstein J Nanotechnol 2020 Oct 19;11:1577-1589.PMID:33134002DOI:10.3762/bjnano.11.140.

Identifying the atomic structure of organic-inorganic interfaces is challenging with current research tools. Interpreting the structure of complex molecular adsorbates from microscopy images can be difficult, and using atomistic simulations to find the most stable structures is limited to partial exploration of the potential energy surface due to the high-dimensional phase space. In this study, we present the recently developed Bayesian Optimization Structure Search (BOSS) method as an efficient solution for identifying the structure of non-planar adsorbates. We apply BOSS with density-functional theory simulations to detect the stable adsorbate structures of (1S)-camphor on the Cu(111) surface. We identify the optimal structure among eight unique types of stable adsorbates, in which camphor chemisorbs via oxygen (global minimum) or physisorbs via hydrocarbons to the Cu(111) surface. This study demonstrates that new cross-disciplinary tools, such as BOSS, facilitate the description of complex surface structures and their properties, and ultimately allow us to tune the functionality of advanced materials.

Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer

FEBS Lett 1997 Oct 6;415(3):253-7.PMID:9357977DOI:10.1016/s0014-5793(97)01135-6.

The crystal structure of cytochrome P-450cam complexed with the enantiomer (1S)-camphor has been solved to 1.8 angstroms resolution and compared with the structure of the (1R)-camphor P-450cam complex. The overall protein structure is the same for both enantiomer complexes. However, the orientation of the substrates in the heme pocket differs. In contrast to (1R)-camphor, the (1S)-enantiomer binds in at least two orientations. The major binding mode of (1S)-camphor resembles the one of the (1R)-enantiomer in that there is a hydrogen bond between Tyr-96 and the quinone group of camphor, and the 10-methyl group points towards the I-helix. The binding differs in that C-5 is not at a position suitable for hydroxylation. In the other orientation (1S)-camphor is not hydrogen bonded, but C-5 is located suitably for hydroxylation.

Structural changes in cytochrome P-450cam effected by the binding of the enantiomers (1R)-camphor and (1S)-camphor

Biochemistry 1996 Nov 12;35(45):14127-38.PMID:8916898DOI:10.1021/bi9527303.

A comparative study of the enantiomeric substrate [(1R)-camphor- and (1S)-camphor)-bound cytochrome P-450cam concerns the spin-state equilibrium, substrate dissociation, the thermal unfolding of the protein structure, and the subconformer equilibria observed in the infrared spectra of the carbon monoxide (CO) complex of cytochrome P-450cam. The behavior of the different conformational equilibria in dependence on temperature, pressure, pH-value, cosolvent, and cation binding led us to suggest that (1S)-camphor is more loosely and less optimally bound in the heme pocket, which facilitates the access of solvent molecules into the heme-iron environment. The spin reaction volume difference measured using the high pressure technique is smaller by 16 +/- 9 cm3/mol for (1S)-camphor-bound P-450cam compared to the (1R)-camphor-bound P-450cam, which might indicate a higher water content in the protein and in the heme environment in the (1S)-camphor complex. The half-transition temperature of the thermal unfolding of 53.8 degrees C for the (1S)-camphor-bound oxidized cytochrome P-450cam is one degree lower than the value for the (1R)-camphor-bound protein (54.8 degrees C). In the reduced, CO-bound form of cytochrome P-450cam at 290 K the (1S)-camphor complex reveals another CO stretch vibration population distribution with slightly higher frequencies [1940.2 cm-1 (major band) and 1946.3 cm-1 (minor band)] compared to the (1R)-camphor complex [1939.7 cm-1 (major band) and 1930 cm-1 (minor band)]. A loosening of the contact between the iron-bound CO ligand and amino acids of the I-helix, probably induced by compensating effects of the increased water content, is suggested. Assuming the carbon monoxide complex as a model for the dioxygen complex, the more loosened binding of (1S)-camphor, therefore the increased water accessibility, and the weaker contact of the iron ligand to the I-helix might explain the higher amount of uncoupling of the cytochrome P-450 reaction cycle compared to that when (1R)-camphor is used as substrate.