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870764-59-3

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870764-59-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 870764-59-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 8,7,0,7,6 and 4 respectively; the second part has 2 digits, 5 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 870764-59:
(8*8)+(7*7)+(6*0)+(5*7)+(4*6)+(3*4)+(2*5)+(1*9)=203
203 % 10 = 3
So 870764-59-3 is a valid CAS Registry Number.

870764-59-3Relevant articles and documents

The role of protecting groups in the formation of organogels through a nano-fibrillar network formed by self-assembling terminally protected tripeptides

Das, Apurba K.,Bose, Partha Pratim,Drew, Michael G.B.,Banerjee, Arindam

, p. 7432 - 7442 (2008/02/05)

A series of eight synthetic self-assembling terminally blocked tripeptides have been studied for gelation. Some of them form gels in various aromatic solvents including benzene, toluene, xylene, and chlorobenzene. It has been found that the protecting groups play an important role in the formation of organogels. It has been observed that, if the C-terminal has been changed from methyl ester to ethyl ester the gelation property does not change significantly (keeping the N-terminal protecting group same), while the change of the protecting group from ethyl ester to isopropyl ester completely abolishes the gelation property. Similarly, keeping the identical C-terminal protecting group (methyl ester) the results of the gelation study indicate that the substitution of N-terminal protection Boc- (tert-butyloxycarbonyl) to Cbz- (benzyloxycarbonyl) does change the gelation property insignificantly, while the change from Boc- to pivaloyl (Piv-) or acetyl (Ac-) group completely eliminates the gelation property. Morphological studies of the dried gels of two of the peptides indicate the presence of an entangled nano-fibrillar network that might be responsible for gelation. FTIR studies of the gels demonstrate that an intermolecular hydrogen bonding network is formed during gelation. Results of X-ray powder diffraction studies for these gelator peptides in different states (dried gels, gel, and bulk solids) reflected that the structure in the wet gel is distinctly different from the dried gel and solid state structures. Single crystal X-ray diffraction studies of a non-gelator peptide, which is structurally similar to the gelator molecules reveal that the peptide forms an antiparallel β-sheet structure in crystals.

Synthesis of a Derivative of the Peptaibol-Antibiotic Trichovirin I 1B by Means of the 'Azirine/Oxazolone Method'

Luykx, Roeland T. N.,Linden, Anthony,Heimgartner, Heinz

, p. 4093 - 4111 (2007/10/03)

According to the earlier published synthesis of the C-terminal nonapeptide of Trichovirin I 1B, Z-Ser(tBu)-Val-Aib-Pro-Aib-Leu-Aib-Pro-Leuol (5), the complete tetradecapeptide Z-Aib-Asn(Trt)-Leu-Aib-Pro-Ser( tBu)-Val-Aib-Pro-Aib-Leu-

Soluble alpha-amino acid salts in acetonitrile: practical technology for the production of some dipeptides.

Palomo, Claudio,Palomo, Antonio L,Palomo, Francisco,Mielgo, Antonia

, p. 4005 - 4008 (2007/10/03)

Alpha-amino acids are soluble in acetonitrile when treated with phosphazene bases. As a result, the protection/deprotection events that are usually required for peptide coupling reactions can be minimized. This is illustrated in the synthesis of the important angiotensin-converting enzyme (ACE) inhibitor enalapril. [reaction: see text]

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