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22802-67-1

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22802-67-1 Usage

General Description

Methyl 5-amino-o-anisate is a chemical compound that is derived from anisole, an aromatic compound found in essential oils. It is a white crystalline powder with a molecular formula C9H11NO3. Methyl 5-amino-o-anisate has a variety of uses, including as an intermediate in the production of pharmaceuticals and as a fragrance ingredient in perfumes and personal care products. It is also used as a raw material in the synthesis of organic compounds, particularly for the manufacture of dyes and pigments. Additionally, it has shown potential as an anti-inflammatory agent in medical research. Overall, methyl 5-amino-o-anisate has multiple applications in various industries and fields.

Check Digit Verification of cas no

The CAS Registry Mumber 22802-67-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,2,8,0 and 2 respectively; the second part has 2 digits, 6 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 22802-67:
(7*2)+(6*2)+(5*8)+(4*0)+(3*2)+(2*6)+(1*7)=91
91 % 10 = 1
So 22802-67-1 is a valid CAS Registry Number.
InChI:InChI=1/C9H11NO3/c1-12-8-4-3-6(10)5-7(8)9(11)13-2/h3-5H,10H2,1-2H3

22802-67-1SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name methyl 5-amino-2-methoxybenzoate

1.2 Other means of identification

Product number -
Other names Methyl 5-amino-2-methoxybenzoate

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:22802-67-1 SDS

22802-67-1Relevant articles and documents

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Kratzl,Vierhapper

, p. 224,227,232 (1971)

-

EIF4E INHIBITORS AND USES THEREOF

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Paragraph 00506; 00522, (2021/09/11)

The present invention provides compounds inhibiting elF4E activity and compositions and methods of using thereof.

Folding and Assembly of Short α, β, ?-Hybrid Peptides: Minor Variations in Sequence and Drastic Differences in Higher-Level Structures

Zhang, Yukun,Zhong, Yulong,Connor, Alan L.,Miller, Daniel P.,Cao, Ruikai,Shen, Jie,Song, Bo,Baker, Erin S.,Tang, Quan,Pulavarti, Surya V.S.R.K.,Liu, Rui,Wang, Qiwei,Lu, Zhong-Lin,Szyperski, Thomas,Zeng, Huaqiang,Li, Xiaopeng,Smith, Richard D.,Zurek, Eva,Zhu, Jin,Gong, Bing

, p. 14239 - 14248 (2019/10/11)

Multilevel protein structures typically involve polypeptides of sufficient lengths. Here we report the folding and assembly of seven short tetrapeptides sharing the same types of α-, β-, and aromatic ?-amino acid residues. These are two sets of hybrid peptides, with three members in one set and four in the other, having complementary hydrogen-bonding sequences that were hypothesized to pair into linear H-bonded duplexes. However, instead of undergoing the anticipated pairing, the initially examined three oligomers, 1 and 2a or 2b, differing only in their central αβ hybrid dipeptide sequence, do not associate with each other and exhibit distinctly different folding behavior. Experiments based on NMR and mass spectrometry, along with computational studies and systematic inference, reveal that oligomer 1 folds into an expanded β-turn containing an unusual hybrid α/β-amino acid sequence composed of glycine and β-alanine, two α- A nd β-amino acid residues that are conformationally most flexible, and peptides 2a and 2b adopt a noncanonical, extended helical conformation and dimerize into double helices undergoing rapid conformational exchange or helix inversion. The different central dipeptide sequences, αβ vs βα, result in drastically different intramolecular H-bonding patterns that are responsible for the observed folding behavior of 1 and 2. The revealed turn and double helix have few natural or synthetic counterparts, and provide novel and unique folding prototypes based on which chiral α- A nd β-amino acids are incorporated. The resultant derivatives 1a, 1b, 2c, and 2d follow the same folding and assembling behavior and demonstrate the generality of this system with the formation of expanded β-turns and double helices with enhanced folding stabilities, hampered helix inversion, as well as defined and dominant helical sense. This work has demonstrated the unique capability of synthetic foldamers in generating structures with fascinating folding and assembling behavior. The revealed systems offer ample opportunity for further structural optimization and applications.

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