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methyl (tert-butoxycarbonyl)-L-tryptophyl-L-tyrosinate is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

72156-63-9

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72156-63-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 72156-63-9 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,2,1,5 and 6 respectively; the second part has 2 digits, 6 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 72156-63:
(7*7)+(6*2)+(5*1)+(4*5)+(3*6)+(2*6)+(1*3)=119
119 % 10 = 9
So 72156-63-9 is a valid CAS Registry Number.

72156-63-9Relevant academic research and scientific papers

Photochemical Chemoselective Alkylation of Tryptophan-Containing Peptides

Laroche, Benjamin,Tang, Xinjun,Archer, Gaétan,Di Sanza, Riccardo,Melchiorre, Paolo

supporting information, p. 285 - 289 (2021/01/26)

We report a photochemical method for the chemoselective radical functionalization of tryptophan (Trp)-containing peptides. The method exploits the photoactivity of an electron donor-acceptor complex generated between the tryptophan unit and pyridinium sal

Copper-Promoted O-Arylation of the Phenol Side Chain of Tyrosine Using Triarylbismuthines

Gagnon, Alexandre,Hébert, Martin,Le Roch, Adrien

supporting information, p. 5363 - 5367 (2020/08/27)

A general method for the O-arylation of the side chain of tyrosine using triarylbismuth reagents is reported. The reaction is mediated by copper diacetate, operates at 50 °C under oxygen in dichloromethane in the presence of pyridine, shows excellent functional group compatibility, and retains the integrity of the stereogenic center. The protocol was used to arylate the tyrosine residue of dipeptides and tripeptides.

Site-selective modification of peptides using rhodium and palladium catalysis: Complementary electrophilic and nucleophilic arylation

Chapman, Christopher J.,Matsuno, Ai,Frost, Christopher G.,Willis, Michael C.

, p. 3903 - 3905 (2008/09/19)

The site-selective modification of peptides containing dehydroalanine, tyrosine and tryptophan residues has been achieved using rhodium catalysed conjugate additions or palladium catalysed aryl-amination and -etherification reactions. The Royal Society of

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