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3017-32-1

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3017-32-1 Usage

General Description

(S)-methyl 2-amino-6-(tert-butoxycarbonylamino)hexanoate is a chemical compound with the molecular formula C11H22N2O4. It is an amino acid derivative with a tert-butoxycarbonyl (Boc) protecting group on the amino group. (S)-methyl 2-amino-6-(tert-butoxycarbonylamino)hexanoate is commonly used as a building block in organic synthesis and as a reagent in peptide chemistry. It is also used in the production of pharmaceuticals and bioactive compounds. Additionally, (S)-methyl 2-amino-6-(tert-butoxycarbonylamino)hexanoate has potential applications in the field of medicinal chemistry, particularly in drug discovery and development. Furthermore, it has been studied for its potential biological activities, including antimicrobial and antitumor properties.

Check Digit Verification of cas no

The CAS Registry Mumber 3017-32-1 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 3,0,1 and 7 respectively; the second part has 2 digits, 3 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 3017-32:
(6*3)+(5*0)+(4*1)+(3*7)+(2*3)+(1*2)=51
51 % 10 = 1
So 3017-32-1 is a valid CAS Registry Number.

3017-32-1Relevant articles and documents

Investigating a Boronate-Affinity-Guided Acylation Reaction for Labelling Native Antibodies

Adak, Avijit K.,Huang, Kuan-Ting,Liao, Chien-Yu,Lee, Yuan-Jung,Kuo, Wen-Hua,Huo, Yi-Ren,Li, Pei-Jhen,Chen, Yi-Ju,Chen, Bo-Shiun,Chen, Yu-Ju,Chu Hwang, Kuo,Wayne Chang, Wun-Shang,Lin, Chun-Cheng

supporting information, (2022/02/22)

The excellent molecular recognition capabilities of monoclonal antibodies (mAbs) have opened up exciting opportunities for biotherapeutic discovery. Taking advantage of the full potential of this tool necessitates affinity ligands capable of conjugating directly with small molecules to a defined degree of biorthogonality, especially when modifying natural Abs. Herein, a bioorthogonal boronate-affinity-based Ab ligand featuring a 4-(dimethylamino)pyridine and an S-aryl thioester to label full-length Abs is reported. The photoactivatable linker in the acyl donor facilitated purification of azide-labelled Ab (N3-Ab) was quantitatively cleaved upon brief exposure to UV light while retaining the original Ab activity. Click reactions enabled the precise addition of biotin, a fluorophore, and a pharmacological agent to the purified N3-Abs. The resulting immunoconjugate showed selectivity against targeted cells. Bioorthogonal traceless design and reagentless purification allow this strategy to be a powerful tool to engineer native antibodies amenable to therapeutic intervention.

KETONE INHIBITORS OF LYSINE GINGIPAIN

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Paragraph 0269, (2018/04/12)

The present invention provides compounds according to Formula (I) as described herein, and their use for inhibiting the lysine gingipain protease (Kgp) from the bacterium Porphyromonas gingivalis. Also described are gingipain activity probe compounds and methods for assaying gingipain activity are also described, as well as methods for the treatment of disorders associated with P. gingivalis infection, including brain disorders such as Alzheimer's disease.

Simple and efficient Fmoc removal in ionic liquid

Di Gioia,Costanzo,De Nino,Maiuolo,Nardi,Olivito,Procopio

, p. 36482 - 36491 (2017/08/02)

A mild method for an efficient removal of the fluorenylmethoxycarbonyl (Fmoc) group in ionic liquid was developed. The combination of a weak base such as triethylamine and [Bmim][BF4] makes the entire system more efficient for the cleavage at room temperature of various amines and amino acid methyl esters in short reaction times. The procedure works well even in the case of N-Fmoc amino acids bearing acid-sensitive protecting groups and of N-alkylated amino acid methyl esters. The solvent-free condition provides a complementary method for Fmoc deprotection in solution phase peptide synthesis and modern organic synthesis.

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