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O-benzylaspartyl-phenylalanine amide is a synthetic chemical compound with the molecular formula C20H22N2O4. It is a derivative of the naturally occurring dipeptide aspartyl-phenylalanine, where the aspartic acid residue is modified with a benzyl group. This modification enhances the stability and bioavailability of the compound, which is often used in pharmaceutical research and development. The compound is known for its potential applications in the treatment of various diseases, including cancer, due to its ability to inhibit certain enzymes and disrupt protein-protein interactions. Its chemical structure and properties make it a subject of interest for medicinal chemistry and drug design, as it can be further modified to improve its therapeutic effects and reduce potential side effects.

5609-55-2

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5609-55-2 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 5609-55-2 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 5,6,0 and 9 respectively; the second part has 2 digits, 5 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 5609-55:
(6*5)+(5*6)+(4*0)+(3*9)+(2*5)+(1*5)=102
102 % 10 = 2
So 5609-55-2 is a valid CAS Registry Number.

5609-55-2Relevant academic research and scientific papers

Microwave-assisted solution phase peptide synthesis in neat water

Mahindra, Amit,Nooney, Karthik,Uraon, Shrikant,Sharma, Krishna K.,Jain, Rahul

, p. 16810 - 16816 (2013/09/23)

An environmentally benign protocol for solution phase peptide synthesis has been developed in neat water using TBTU/HOBt/DIEA as a coupling combination under microwave irradiation. Key features of this procedure are the replacement of commonly used toxic organic solvents like DMF and NMP, the use of lower amounts of reactants, compatibility with both N-α-Boc- and N-α-Fmoc-protected amino acids and all commonly used side-chain protective groups, short reaction time, and racemization-free synthesis in high yield and purity. The Royal Society of Chemistry 2013.

Development of peptide 3D structure mimetics: Rational design of novel peptoid cholecystokinin receptor antagonists

Low,Black,Broughton,Buck,Davies,Dunstone,Hull,Kalindjian,McDonald,Pether,Shankley,Steel

, p. 3505 - 3517 (2007/10/03)

The two hormones cholecystokinin and gastrin share the same C-terminal sequence of amino acids, namely Gly29-Trp30-Met31-Asp32-Phe33-NH2. Nevertheless, this congruence has not precluded usi

PAPAIN-CATALYZED FRAGMENT SYNTHESIS OF PROTECTED CHOLECYSTOKININ DERIVATIVES

Cerovsky, Vaclav,Pirkova, Jana,Majer, Pavel,Slaninova, Jirina,Hlavacek, Jan

, p. 1873 - 1882 (2007/10/02)

Sodium salts of methyl esters of N-tert-butyloxycarbonyl-β-tert-butylaspartyl-O4-sulfotyrosine (II) or N-tert-butyloxycarbonyl-O4-sulfotyrosine (III) were condensed with amino components derived from peptide amides IVb-IVe and IVg (simulating the carboxy-terminal part of cholecystokinin) under catalysis with papain.Rates and yields of conversion of these peptides to the corresponding derivatives Ib-If were compared with the results reported previously for analogous papain-catalyzed fragment synthesis of the protected carboxy-terminal octapeptide of cholecystokinin Ia.In the condensation reactions with the individual amino components quantitative changes were observed in the ability of papain to catalyze the peptide bond synthesis which appeared as differences in the maximum yield (and the time required for achieving it) of the condensation reaction, monitored by HLPC.The observed differences are related not only with the distance of the amino acid substitution from the P'1 subsite in the given amino component but also with the side-chain structure of the substituting amino acid.

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