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87694-55-1

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87694-55-1 Usage

General Description

TERT-BUTYL [(1S,3S)-1-FORMYL-3-METHYLPENTYL]CARBAMATE is a chemical compound with the molecular formula C14H27NO3. It is a carbamate derivative that consists of a tert-butyl group, a formyl group, and a methylpentyl group linked to a carbamate functional group. TERT-BUTYL [(1S,3S)-1-FORMYL-3-METHYLPENTYL]CARBAMATE is commonly used as a reagent in organic synthesis, particularly in the preparation of pharmaceuticals and agrochemicals. The presence of the formyl group makes it a versatile building block in the creation of various complex molecules. TERT-BUTYL [(1S,3S)-1-FORMYL-3-METHYLPENTYL]CARBAMATE is typically colorless and odorless, making it easy to handle in laboratory settings.

Check Digit Verification of cas no

The CAS Registry Mumber 87694-55-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,7,6,9 and 4 respectively; the second part has 2 digits, 5 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 87694-55:
(7*8)+(6*7)+(5*6)+(4*9)+(3*4)+(2*5)+(1*5)=191
191 % 10 = 1
So 87694-55-1 is a valid CAS Registry Number.

87694-55-1SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 18, 2017

Revision Date: Aug 18, 2017

1.Identification

1.1 GHS Product identifier

Product name N-(t-butoxycarbonyl)-isoleucine aldehyde

1.2 Other means of identification

Product number -
Other names N–Boc–L–isoleucinal

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:87694-55-1 SDS

87694-55-1Relevant articles and documents

Elastase Inhibitor Cyclotheonellazole A: Total Synthesis and in Vivo Biological Evaluation for Acute Lung Injury

Cui, Yingjun,Zhang, Mengyi,Xu, Honglei,Zhang, Tingrong,Zhang, Songming,Zhao, Xiuhe,Jiang, Peng,Li, Jing,Ye, Baijun,Sun, Yuanjun,Wang, Mukuo,Deng, Yangping,Meng, Qing,Liu, Yang,Fu, Qiang,Lin, Jianping,Wang, Liang,Chen, Yue

, p. 2971 - 2987 (2022/01/27)

Acute lung injury/acute respiratory distress syndrome (ALI/ARDS) is one of the most common complications in COVID-19. Elastase has been recognized as an important target to prevent ALI/ARDS in the patient of COVID-19. Cyclotheonellazole A (CTL-A) is a nat

Small molecule peptidomimetic trypsin inhibitors: validation of an EKO binding mode, but with a twist

Burgess, Kevin,Joy, Shaon,Laganowsky, Arthur,Lyu, Rui-Liang,Packianathan, Charles

supporting information, p. 2075 - 2080 (2022/03/31)

Examination of a series of naturally-occurring trypsin inhibitor proteins, led to identification of a set of three residues (which we call the “interface triplet”) to be determinant of trypsin binding affinity, hence excellent templates for small molecule mimicry. Consequently, we attempted to use the Exploring Key Orientation (EKO) strategy developed in our lab to evaluate small molecules that mimic the interface triplet regions of natural trypsin inhibitors, and hence potentially might bind and inhibit the catalytic activity of trypsin. A bis-triazole scaffold (“TT-mer”) was the most promising of the molecules evaluated in silico. Twelve such compounds were synthesized and assayed against trypsin, among which the best showed a Kd of 2.1 μM. X-ray crystallography revealed a high degree of matching between an illustrative TT-mer's actual binding mode and that of the mimics that overlaid the interface triplet in the crystal structure. Deviation of the third side chain from the PPI structure seems to be due to alleviation of an unfavorable dipole-dipole interaction in the small molecule's actual bound conformation.

Synthesis, SAR and biological studies of sugar amino acid-based almiramide analogues: N-methylation leads the way

Das, Dipendu,Khan, Hina P. A.,Shivahare, Rahul,Gupta, Suman,Sarkar, Jayanta,Siddiqui, Mohd. Imran,Ampapathi, Ravi Sankar,Chakraborty, Tushar Kanti

, p. 3337 - 3352 (2017/04/21)

Leishmaniasis, caused by the protozoan parasites of the genus Leishmania, is one of the most neglected diseases endemic in many continents posing enormous global health threats and therefore the discovery of new antileishmanial compounds is of utmost urgency. The antileishmanial activities of a library of sugar amino acid-based linear lipopeptide analogues were examined with the aim to identify potential drug candidates to treat visceral leishmaniasis. It was found that among the synthesized analogues, most of the permethylated compounds exhibited more activity in in vitro studies against intra-macrophagic amastigotes than the non-methylated analogues. SAR and NMR studies revealed that introduction of the N-methyl groups inhibited the formation of any turn structure in these molecules, which led to their improved activities.

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