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Z-Gly-Gly-Phe-Leu-O-t-butyl is a peptide compound consisting of a sequence of five amino acids: glycine (Gly), glycine (Gly), phenylalanine (Phe), leucine (Leu), and a terminal t-butyl group. The "Z" prefix indicates the presence of a carbobenzyloxy (Cbz) protecting group on the N-terminus, which is commonly used in peptide synthesis to prevent unwanted side reactions. This specific peptide sequence is of interest in the field of chemistry and biochemistry, as it can be used as a building block for the synthesis of larger peptides or proteins, or as a model compound for studying peptide interactions and folding. The t-butyl group at the C-terminus serves as a protecting group, which can be removed under acidic conditions to yield the free peptide.

77426-95-0

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77426-95-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 77426-95-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,7,4,2 and 6 respectively; the second part has 2 digits, 9 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 77426-95:
(7*7)+(6*7)+(5*4)+(4*2)+(3*6)+(2*9)+(1*5)=160
160 % 10 = 0
So 77426-95-0 is a valid CAS Registry Number.

77426-95-0Downstream Products

77426-95-0Relevant academic research and scientific papers

METHOD FOR PRODUCING AMIDE COMPOUND

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Paragraph 0102-0103, (2020/05/14)

Provided is a novel method for producing amide compounds at high stereochemical selectivities. The method according to the present invention for producing amide compounds is provided with an amidation step for reacting, in the presence of a catalyst compr

Substrate-directed lewis-acid catalysis for peptide synthesis

Muramatsu, Wataru,Hattori, Tomohiro,Yamamoto, Hisashi

supporting information, p. 12288 - 12295 (2019/08/20)

A Lewis-acid-catalyzed method for the substrate-directed formation of peptide bonds has been developed, and this powerful approach is utilized for the new "remote" activation of carboxyl groups under solvent-free conditions. The presented method has the following advantages: (1) the high-yielding peptide synthesis uses a tantalum catalyst for any amino acids; (2) the reaction proceeds without any racemization; (3) the new substrate-directed chemical ligation using the titanium catalyst is applicable to convergent peptide synthesis. These advantages overcome some of the unresolved problems in classical peptide synthesis.

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