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"α-(carbobenzyloxy)nitroarginyl-ε-(carbobenzyloxy)lysylaspartic acid β-benzyl ester" is a complex peptide derivative with a molecular structure that features a nitroarginine residue at the α-position, a lysine residue at the ε-position, and an aspartic acid residue. The carbobenzyloxy (Cbz) groups are protecting groups used in peptide synthesis to prevent unwanted side reactions, particularly the reaction of the amino group with other functional groups. The β-benzyl ester group is another protecting group that shields the carboxylic acid group, which is crucial for maintaining the integrity of the peptide during synthesis. This specific chemical is often used in the synthesis of larger peptides or proteins, where the protecting groups are later removed to yield the desired peptide sequence. The complexity of this molecule highlights the精细的化学合成技术 used in the preparation of biologically active peptides.

72210-37-8

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72210-37-8 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 72210-37-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,2,2,1 and 0 respectively; the second part has 2 digits, 3 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 72210-37:
(7*7)+(6*2)+(5*2)+(4*1)+(3*0)+(2*3)+(1*7)=88
88 % 10 = 8
So 72210-37-8 is a valid CAS Registry Number.

72210-37-8Relevant academic research and scientific papers

Stabilized analogs of thymopentin. 1. 4,5-Ketomethylene pseudopeptides

DeGraw, Joseph I.,Almquist, Ronald G.,Hiebert, Charles K.,Colwell, William T.,Crase, Jac,Hayano, Takeshi,Judd, Amrit K.,Dousman, Linda,Smith, R. Lane,Waud, William R.,Uchida, Itsuo

, p. 2386 - 2397 (2007/10/03)

The pentapeptide, thymopentin (Arg1-Lys2-Asp3-Val4-Tyr5) is known for its activity as an immunomodulating drug, but with limited half-life in plasma. In this first paper of a series of three studies, the synthesis of analogs stabilized at the peptide bond between the C-terminal amino acids via insertion of a ketomethylene moiety is described. N-Blocked pseudopeptides containing Val(k)Phe, Ala(k)Phe, and Val(k)Val units were prepared and attached to chloromethyl Merrifield resin via the carboxy terminal. Removal of the N-BOC group by trifluoroacetic acid was followed by sequential coupling with N-BOC dipeptides of aspartic acid to yield resin-bound N-BOC pseudotetrapeptides. Removal of N-BOC and coupling with N-BOC-r-N- tosylarginine followed by total cleavage of blocking groups and resin by HF afforded the target pseudopentapeptides. The analogs were found to compete favorably with thymopentin for binding to CEM cells, but binding was reduced by about 20-30% on average. All analogs showed significant enhancement of half-life versus thymopentin in mouse serum, but most showed only modest improvement in human serum. Insertion of proline or norleucine at position 2 in the chain caused a substantial increase in half-life (3-4-fold), while N- methylnorleucine conferred complete stability in the analogs.

SYNTHETIC APPROACHES FOR THYMOPENTIN (TP-5) USING THE "IN SITU" SILYLATION STRATEGY WITH TRIMETHYLSILYL CYANIDE

Becu, Fr.,Becu, Chr.,Anteunis, M. J. O.

, p. 15 - 23 (2007/10/02)

The synthesis of the pentapeptide TP-5 has been considered as a test case for the "in situ" silylating strategy, using trimethylsilyl cyanide, because of the nature of the involved residues.Thus orthogonal lateral protections for Arg, Lys and Asp are need

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