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79009-37-3

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79009-37-3 Usage

Description

H-THR-NHME is a peptide chemical compound that consists of the amino acid threonine (THR) linked to a methyl group (NHME) through a peptide bond. Threonine is a polar amino acid that is essential for the human diet and plays a crucial role in protein synthesis and the formation of the structural and functional components of cells. The addition of the methyl group in H-THR-NHME introduces a hydrophobic property to the compound, which may affect its solubility and interactions with other molecules. This unique combination of properties makes H-THR-NHME a promising candidate for the development of novel peptides with specific properties for various biomedical and therapeutic applications.

Uses

Used in Pharmaceutical Industry:
H-THR-NHME is used as a building block for the development of novel peptides with specific properties for various pharmaceutical applications. The hydrophobic property introduced by the methyl group in H-THR-NHME can potentially enhance the bioavailability and stability of the peptides, making them more effective in drug delivery and targeting.
Used in Cosmetic Industry:
H-THR-NHME is used as an ingredient in cosmetic products for its potential moisturizing and skin conditioning properties. The polar nature of threonine and the hydrophobic property of the methyl group in H-THR-NHME can contribute to the overall effectiveness of cosmetic formulations, providing hydration and improving skin texture.
Used in Food Industry:
H-THR-NHME can be used as a functional ingredient in the food industry, where its unique combination of polar and hydrophobic properties can contribute to the development of innovative food products with improved taste, texture, and shelf life.
Used in Research and Development:
H-THR-NHME serves as a valuable research tool for scientists and researchers working in the fields of biochemistry, molecular biology, and drug discovery. Its unique properties can be utilized to study the interactions between peptides and other biomolecules, as well as to develop new therapeutic agents and diagnostic tools.

Check Digit Verification of cas no

The CAS Registry Mumber 79009-37-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,9,0,0 and 9 respectively; the second part has 2 digits, 3 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 79009-37:
(7*7)+(6*9)+(5*0)+(4*0)+(3*9)+(2*3)+(1*7)=143
143 % 10 = 3
So 79009-37-3 is a valid CAS Registry Number.

79009-37-3SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 15, 2017

Revision Date: Aug 15, 2017

1.Identification

1.1 GHS Product identifier

Product name H-THR-NHME

1.2 Other means of identification

Product number -
Other names allo-Threonine N-methyl amide

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:79009-37-3 SDS

79009-37-3Relevant articles and documents

SPIRO-LACTAM NMDA MODULATORS AND METHODS OF USING SAME

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Page/Page column 54; 56; 57, (2018/03/28)

Disclosed are compounds having potency in the modulation of NMDA receptor activity. Such compounds can be used in the treatment of conditions such as depression and related disorders. Orally delivered formulations and other pharmaceutically acceptable delivery forms of the compounds, including intravenous formulations, are also disclosed.

Non-natural amino acids as modulating agents of the conformational space of model glycopeptides

Fernandez-Tejada, Alberto,Corzana, Francisco,Busto, Jesus H.,Jimenez-Oses, Gonzalo,Peregrina, Jesus M.,Avenoza, Alberto

supporting information; experimental part, p. 7042 - 7058 (2009/07/25)

The synthesis and conformational analysis in aqueous solution of different α-methyl-α-amino acid di-amides, derived from serine, threonine, β-hydroxycyclobutane-α-amino acids, and their corresponding model β-O-glucopeptides, are reported. The study reveals that the presence of an α-methyl group forces the model peptides to adopt helix-like conformations. These folded conformations are especially significant for cyclobutane derivatives. Interestingly, this feature was also observed in the corresponding model glucopeptides, thus indicating that the α-methyl group and not the β-O-glucosylation process largely determines the conformational preference of the backbone in these structures. On the other hand, atypical conformations of the glycosidic linkage were experimentally determined. Therefore, when a methyl group was located at the Cβ atom with an R configuration, the glycosidic linkage was rather rigid. Never-theless, when the S configuration was displayed, a significant degree of flexibility was observed for the glycosidic linkage, thus showing both alternate and eclipsed conformations of the ψb dihedral angle. In addition, some derivatives exhibited an unusual value for the Φ2 angle, which was far from a value of -60° expected for a conventional β-O-glycosidic linkage. In this sense, the different conformations exhibited by these molecules could be a useful tool in obtaining systems with conformational preferences "a la carte".

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