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Carbamic acid, [(chloromethoxyphosphinyl)methyl]-, phenylmethyl ester is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

80556-22-5

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80556-22-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 80556-22-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,0,5,5 and 6 respectively; the second part has 2 digits, 2 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 80556-22:
(7*8)+(6*0)+(5*5)+(4*5)+(3*6)+(2*2)+(1*2)=125
125 % 10 = 5
So 80556-22-5 is a valid CAS Registry Number.

80556-22-5Relevant academic research and scientific papers

Reactive species formed from N-benzyloxycarbonyl α-aminophosphonochloridates and triethylamine: Probable identity and implications for synthesis

Cullis, Paul M.,Harger, Martin J. P.

, p. 458 - 459 (2002)

The sterically congested phosphonochloridate BnOCONHCMe2P(O)(OMe)Cl reacts rapidly with Et3N to give what is thought to be an oxazaphospholine oxide 7 (and Et3NHCl); unhindered BnOCONHCH2P(O)(OMe)Cl seems to rea

Rational Design of Thermodynamic and Kinetic Binding Profiles by Optimizing Surface Water Networks Coating Protein-Bound Ligands

Krimmer, Stefan G.,Cramer, Jonathan,Betz, Michael,Fridh, Veronica,Karlsson, Robert,Heine, Andreas,Klebe, Gerhard

, p. 10530 - 10548 (2016/12/16)

A previously studied congeneric series of thermolysin inhibitors addressing the solvent-accessible S2′ pocket with different hydrophobic substituents showed modulations of the surface water layers coating the protein-bound inhibitors. Increasing stabilization of water molecules resulted in an enthalpically more favorable binding signature, overall enhancing affinity. Based on this observation, we optimized the series by designing tailored P2′ substituents to improve and further stabilize the surface water network. MD simulations were applied to predict the putative water pattern around the bound ligands. Subsequently, the inhibitors were synthesized and characterized by high-resolution crystallography, microcalorimetry, and surface plasmon resonance. One of the designed inhibitors established the most pronounced water network of all inhibitors tested so far, composed of several fused water polygons, and showed 50-fold affinity enhancement with respect to the original methylated parent ligand. Notably, the inhibitor forming the most perfect water network also showed significantly prolonged residence time compared to the other tested inhibitors.

Intramolecular nucleophilic catalysis and the exceptional reactivity of N-benzyloxycarbonyl α-aminophosphonochloridates

Cullis, Paul M.,Harger, Martin J.P.

, p. 1538 - 1543 (2007/10/03)

The intramolecular nucleophilic catalysis and the exceptional reactivity of N-benzyloxycarbonyl α-aminophosphonochloridates were discussed. It was found that N-benzyloxycarbonyl derivatives of α-aminophosphonochloridates were highly reactive because of in

Differential binding energy: A detailed evaluation of the influence of hydrogen-bonding and hydrophobic groups on the inhibition of thermolysin by phosphorus-containing inhibitors

Morgan, Bradley P.,Scholtz, John M.,Ballinger, Marcus D.,Zipkin, Ilan D.,Bartlett, Paul A.

, p. 297 - 307 (2007/10/02)

Two series of phosphorus-containing peptide analogues, 3 (CbZ-Gly-ψ(PO2-CH2)Leu-Xaa) and 4 (Cbz-Gly-ψ-(PO2-NH)Leuψ[CO2]Xaa), have been synthesized and evaluated as inhibitors of the zinc en

AN ANALYSIS OF THE ENZYME-INHIBITOR BINDING INTERACTIONS FOR PHOSPHONIC ACID TRANSITION STATE ANALOGS OF THERMOLYSIN

Bartlett, Paul A.,Marlowe, Charles K.

, p. 537 - 544 (2007/10/02)

Potent inhibitors of the zinc endopeptidase thermolysin are produced on replacement of the scissile peptide linkage with phosphonamidate or phosphonate ester moieties.These inhibitors have been shown to be transition state analogs, and a comparison betwee

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