40738-21-4

Usage

Uses

Used in Pharmaceutical Development:
H-THR(TBU)-NH2 HCL is used as a building block in the synthesis of peptides for the development of pharmaceuticals. Its protected amino group allows for controlled peptide synthesis, facilitating the creation of complex molecular structures with specific therapeutic properties.
Used in Biochemical Research:
In the field of biochemical research, H-THR(TBU)-NH2 HCL is utilized as a starting material for the synthesis of various bioactive peptides and proteins. Its protected structure enables researchers to explore the properties and functions of these molecules in a controlled manner.
Used in Peptide Synthesis:
H-THR(TBU)-NH2 HCL is used as a key component in peptide synthesis, where its protected amino group allows for the stepwise assembly of peptide chains. This controlled synthesis is crucial for the production of peptides with specific sequences and functions, which can be used in various applications, such as drug development, diagnostics, and therapeutics.
Used in Chemical Synthesis:
In chemical synthesis, H-THR(TBU)-NH2 HCL serves as a versatile building block for the creation of more complex organic molecules. Its protected structure allows for selective reactions and modifications, enabling the synthesis of a wide range of compounds with diverse properties and applications.
Overall, H-THR(TBU)-NH2 HCL is a valuable compound in various industries, including pharmaceuticals, biochemical research, and chemical synthesis, due to its unique properties and applications in the synthesis of peptides and complex molecules.

Upstream product

• 71989-35-0 Fmoc-Thr(tBu)-OH 

Relevant academic research and scientific papers

PROCESS FOR PREPARATION OF LANREOTIDE ACETATE

The invention relates to an improved method for the solution phase synthesis of Lanreotide acetate (1) comprising coupling of two suitably protected tetrapeptide fragments wherein the threonine hydroxyl is protected, to give an octapeptide, which on deprotection, oxidation, followed by treatment with acetic acid provides Lanreotide acetate (1) having desired purity.

Development and evaluation of novel phosphotyrosine mimetic inhibitors targeting the Src homology 2 domain of signaling lymphocytic activation molecule (SLAM) associated protein

Specific interactions between Src homology 2 (SH2) domain-containing proteins and the phosphotyrosine-containing counterparts play significant role in cellular protein tyrosine kinase (PTK) signaling pathways. The SH2 domain inhibitors could potentially serve as drug candidates in treating human diseases. Here we have incorporated a novel phosphotyrosine mimetic, which is an unusual amino acid carrying a cyclosaligenyl (cycloSal) phosphodiester moiety, into dipeptides to investigate the inhibitory effect on SH2 domain-containing proteins. A plate-based assay was also established to screen for inhibitors that disrupt the interaction between a phosphopeptide of SLAM (signaling lymphocytic activation molecule) and its interacting protein SAP (SLAM-associated protein). We identified a number of inhibitors with IC50 values in the range of 17-35 μM, implying that the cycloSal phosphodiester-carrying amino acid could mimic the phosphotyrosyl residue. Our results also raise the possibility of integrating the newly developed phosphotyrosine mimetic moiety into inhibitors designed for other SH2 domain-containing proteins.

Partially retro-inverted tuftsin analogues, method for the preparation thereof and pharmaceutical compositions containing them

New partially retro-inverted tuftsin analogues of general formula I STR1 wherein R represents the side-chain of the amino acids threonine, methionine or leucine R1 represents the side-chain of the amino acids lysine or arginine R2 is hydrogen or a metabolically labile acyl group, all the asymmetric carbon atoms are either of the S- or R-configuration, or, alternatively, the first, third, and fourth asymmetric carbons, starting from the N-terminal residue, are of the S-configuration while the second one is of the R- or (R,S)-configuration, and the corresponding pharmacologically acceptable salts, esters and amides. The new compounds which share the same pharmacological properties of tuftsin, are much more stable toward the enzymatic degradation than the parent molecule.

Partially retro-inverted tuftsin analogues, method for the preparation thereof and pharmaceutical compositions containing them

New partially retro-inverted tuftsin analogues of general formula I wherein, R represents the side-chain of the amino acids threonine, methionine or leucine, R1 represents the side-chain of the amino acids lysine or arginine, R2 is hydrogen or a metabolically labile acyl group,all the asymmetric carbon atoms are either of the S- or R-configuration, or, alternatively, the first, third, and fourth asymmetric carbons, starting from the N-terminal residue, are of the S-configuration while the second one is of the R- or (R,S)-configuration, and the corresponding pharmacologically acceptable salts, esters and amides. The new compounds which share the same pharmacological properties of tuftsin, are much more stable toward the enzymatic degradation than the parent molecule.