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Glycine, N-glycyl-, phenylmethyl ester, also known as N-phenylmethoxycarbonylglycine or Z-glycine, is a chemical compound with the molecular formula C10H11NO4. It is a derivative of glycine, an amino acid, where the amino group is protected by a phenylmethyl ester (Z) group. Glycine, N-glycyl-, phenylmethyl ester is widely used in peptide synthesis as a protecting group for the amino group, preventing unwanted side reactions during the formation of peptide bonds. The Z group can be selectively removed under mild acidic conditions, allowing for the subsequent coupling of the deprotected amino acid with another amino acid. This makes Glycine, N-glycyl-, phenylmethyl ester an essential component in the synthesis of various peptides and proteins, particularly in solid-phase peptide synthesis techniques.

1842-55-3

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1842-55-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1842-55-3 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,8,4 and 2 respectively; the second part has 2 digits, 5 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 1842-55:
(6*1)+(5*8)+(4*4)+(3*2)+(2*5)+(1*5)=83
83 % 10 = 3
So 1842-55-3 is a valid CAS Registry Number.

1842-55-3Relevant academic research and scientific papers

Selective removal of fluorenylmethoxycarbonyl (FMOC) groups under mild conditions

Jiang,Li,Joullie

, p. 187 - 195 (1994)

N-Fluorenylmethoxycarbonyl groups may be removed by potassium fluoride/18- crown-6 in the presence of methyl, ethyl, tert-butyl, benzyl, and p- methoxybenzyl esters.

Development of supramolecular organo-gel based on tripeptide skeletons

Azuma, Eriko,Kuramochi, Kouji,Tsubaki, Kazunori

body text, p. 680 - 684 (2010/07/15)

Boc-Ser-Val-Gly-OCH2Ph (31) showed high gelation abilities in the aromatic solvents, particularly in toluene. The minimum gelation concentration of 31 in toluene was 10 mg/ml, suggesting that 2500 molecules of toluene were immobilized by each m

A templating approach for monodisperse self-assembled organic nanostructures

Bull, Steve R.,Palmer, Liam C.,Fry, Nathaniel J.,Greenfield, Megan A.,Messmore, Benjamin W.,Meade, Thomas J.,Stupp, Samuel I.

, p. 2742 - 2743 (2008/09/20)

The precise structural control is known for self-assembly into closed spherical structures (e.g., micelles), but similar control of open structures is much more challenging. Inspired by natural tobacco mosaic virus, we present the use of a rigid-rod template to control the size of a one-dimensional self-assembly. We believe that this strategy is novel for organic self-assembly and should provide a general approach to controlling size and dimension. Copyright

Thioamides: Synthesis, stability, and immunological activities of thioanalogues of imreg. Preparation of new thioacylating agents using fluorobenzimidazolone derivatives

Zacharie, Boulos,Lagraoui, Mouna,Dimarco, Marika,Penney, Christopher L.,Gagnon, Lyne

, p. 2046 - 2052 (2007/10/03)

Imreg (Tyr1-Gly2-Gly3) is a well-known immunostimulant. However, it possesses a short half-life. Stabilized analogues of Imreg were prepared by a regioselective insertion in which peptide bonds at position 1,2 or 2,3 were

The L-Proline Residue as a 'Break-point' in Metal - Peptide Systems

Pettit, Leslie D.,Steel, Ian,Formicka-Kozlowska, Grazyna,Tatarowski, Tomasz,Bataille, Michael

, p. 535 - 540 (2007/10/02)

Results are reported of a potentiometric and spectrophotometric study of the H+ and Cu2+ complexes of the tetrapeptides X-Gly-Gly-Gly, Gly-X-Gly-Gly, Gly-Gly-X-Gly, and Gly-Gly-Gly-X where X is the proline (Pro) and sarcosine (Sar) residue (Gly=glycine).All the tetrapeptides (HL) form the series of complexes , -1L>, -2L>, and -3L> (charges omitted).The ligands Gly-X-Gly-Gly also form the bis-complex, .When inserted in a peptide chain the Pro and Sar residues cannot co-ordinate to Cu2+ through their peptide nitrogens since they do not possess ionizable protons.In addition the Pro residue tends to force the peptide chain to form a 'β-turn' and so adopt a 'bent' conformation.These studies demonstrate the formation of a large chelate ring when tetrapeptides containing Pro (and , to a smaller extent, Sar) in the second or third positions co-ordinate to Cu2+.This ring spans the terminal residues of the peptide chain and locks the peptide into a 'bent' or 'horse-shoe' shaped conformation.Cu2+ could therefore play an important role in activating oligopeptides (e.g. neuropeptides) containing proline.

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