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1400790-68-2

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1400790-68-2 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1400790-68-2 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,4,0,0,7,9 and 0 respectively; the second part has 2 digits, 6 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 1400790-68:
(9*1)+(8*4)+(7*0)+(6*0)+(5*7)+(4*9)+(3*0)+(2*6)+(1*8)=132
132 % 10 = 2
So 1400790-68-2 is a valid CAS Registry Number.

1400790-68-2Downstream Products

1400790-68-2Relevant academic research and scientific papers

Submonomer synthesis of a hybrid peptoid-azapeptoid library

Sarma, Bani Kanta,Kodadek, Thomas

, p. 558 - 564 (2012)

We recently reported efficient conditions for the synthesis of N-azapeptoid libraries via the typical submonomer strategy of peptoid synthesis but that substitutes N-acyl hydrazides for primary amines as submonomers. Unfortunately, this approach is not applicable to the synthesis of mixed azapeptoid-peptoid libraries. When an oligomer containing an N-terminal side chain derived from an acyl hydrazide is bromoacetylated and treated with a primary amine, a chain-terminating intramolecular ring-closure to form an oxadiazinone competes with the desired displacement of the bromide by the amine. Here we overcome this limitation and demonstrate that a hybrid peptoid-azapeptoid library derived from primary amines, acyl hydrazides, carbazates, and semicarbazides can be made efficiently using standard peptoid submonomer chemistry. We find that the unwanted, chain-terminating cyclization reaction is competitive with chain extension only when aryl acyl hydrazides are present. Alkyl or heteroaromatic acyl hydrazides do not cyclize under the conditions used for peptoid-azapeptoid synthesis. We also find that carbazates and semicarbazides work well for chain extension. Using primary amines, acyl hydrazides, carbazates, and semicarbazides as submonomers, a high-quality one bead one compound library of tetramers suitable for screening against protein targets was made by split and pool synthesis.

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