L-Threonine methylamide
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L-Threonine methylamide

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Category
L-Amino Acids
Catalog number
BAT-003930
CAS number
79009-37-3
Molecular Formula
C5H12N2O2
Molecular Weight
132.16
L-Threonine methylamide
IUPAC Name
(2S,3R)-2-amino-3-hydroxy-N-methylbutanamide
Synonyms
L-Thr-NHMe; allo-Threonine N-methyl amide; THREONINE-NHME; L-THREONINE METHYLAMIDE; L-THREONINE METHYLAMIDE HYDROCHLORIDE
Appearance
Off-white solid
Purity
≥ 95%
Melting Point
62-64 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C5H12N2O2/c1-3(8)4(6)5(9)7-2/h3-4,8H,6H2,1-2H3,(H,7,9)/t3-,4+/m1/s1
InChI Key
NHXXBNOVHYPMHZ-DMTCNVIQSA-N
Canonical SMILES
CC(C(C(=O)NC)N)O
1. Growth differentiation factor 15 stimulates rapamycin-sensitive ovarian cancer cell growth and invasion
Samantha E Griner, Jayashree P Joshi, Rita Nahta Biochem Pharmacol. 2013 Jan 1;85(1):46-58. doi: 10.1016/j.bcp.2012.10.007. Epub 2012 Oct 17.
Identification of novel molecular markers and therapeutic targets may improve survival rates for patients with ovarian cancer. In the current study, immunohistochemical (IHC) analysis of two human ovarian tumor tissue arrays showed high staining for GDF15 in a majority of tissues. Exogenous stimulation of ovarian cancer cell lines with recombinant human GDF15 (rhGDF15) or stable over-expression of a GDF15 expression plasmid promoted anchorage-independent growth, increased invasion, and up-regulation of matrix metalloproteinases (MMPs) and vascular endothelial growth factor (VEGF). MMP inhibition suppressed GDF15-mediated invasion. In addition, IHC analysis of human ovarian tumor tissue arrays indicated that GDF15 expression correlated significantly with high MMP2 and MMP9 expression. Exogenous and endogenous GDF15 over-expression stimulated phosphorylation of p38, Erk1/2, and Akt. Pharmacologic inhibition of p38, MEK, or PI3K suppressed GDF15-stimulated growth. Further, proliferation, growth, and invasion of GDF15 stable clones were blocked by rapamycin. IHC analysis demonstrated significant correlation between GDF15 expression and phosphorylation of mTOR. Finally, knockdown of endogenous GDF15 or neutralization of secreted GDF15 suppressed invasion and growth of a GDF15-over-expressing ovarian cancer cell line. These data indicate that GDF15 over-expression, which occurred in a majority of human ovarian cancers, promoted rapamycin-sensitive invasion and growth of ovarian cancer cells. Inhibition of mTOR may be an effective therapeutic strategy for ovarian cancers that over-express GDF15. Future studies should examine GDF15 as a novel molecular target for blocking ovarian cancer progression.
2. Synthesis and conformational preferences of short analogues of antifreeze glycopeptides (AFGP)
Małgorzata Urbańczyk, Michał Jewgiński, Joanna Krzciuk-Gula, Jerzy Góra, Rafał Latajka, Norbert Sewald Beilstein J Org Chem. 2019 Jul 16;15:1581-1591. doi: 10.3762/bjoc.15.162. eCollection 2019.
Antifreeze glycoproteins are a class of biological agents which enable living at temperatures below the freezing point of the body fluids. Antifreeze glycopeptides usually consist of repeating tripeptide unit (-Ala-Ala-Thr*-), glycosylated at the threonine side chain. However, on the microscopic level, the mechanism of action of these compounds remains unclear. As previous research has shown, antifreeze activity of antifreeze glycopeptides strongly relies on the overall conformation of the molecule as well an on the stereochemistry of amino acid residues. The desired monoglycosylated analogues with acetylated amino termini and the carboxy termini in form of N-methylamide have been synthesized. Conformational nuclear magnetic resonance (NMR) studies of the designed analogues have shown a strong influence of the stereochemistry of amino acid residues on the peptide chain stability, which could be connected to the antifreeze activity of these compounds. A better understanding of the mechanism of action of antifreeze glycopeptides would allow applying these materials, e.g., in food industry and biomedicine.
3. Formation and dissociation of phosphorylated peptide radical cations
Ricky P W Kong, Quan Quan, Qiang Hao, Cheuk-Kuen Lai, Chi-Kit Siu, Ivan K Chu J Am Soc Mass Spectrom. 2012 Dec;23(12):2094-101. doi: 10.1007/s13361-012-0479-7. Epub 2012 Sep 12.
In this study, we generated phosphoserine- and phosphothreonine-containing peptide radical cations through low-energy collision-induced dissociation (CID) of the ternary metal-ligand phosphorylated peptide complexes [Cu(II)(terpy)(p)M](·2+) and [Co(III)(salen)(p)M](·+) [(p)M: phosphorylated angiotensin III derivative; terpy: 2,2':6',2''-terpyridine; salen: N,N'-ethylenebis(salicylideneiminato)]. Subsequent CID of the phosphorylated peptide radical cations ((p)M(·+)) revealed fascinating gas-phase radical chemistry, yielding (1) charge-directed b- and y-type product ions, (2) radical-driven product ions through cleavages of peptide backbones and side chains, and (3) different degrees of formation of [M - H(3)PO(4)](·+) species through phosphate ester bond cleavage. The CID spectra of the (p)M(·+) species and their non-phosphorylated analogues featured fragment ions of similar sequence, suggesting that the phosphoryl group did not play a significant role in the fragmentation of the peptide backbone or side chain. The extent of neutral H(3)PO(4) loss was influenced by the peptide sequence and the initial sites of the charge and radical. A preliminary density functional theory study, at the B3LYP 6-311++G(d,p) level of theory, of the neutral loss of H(3)PO(4) from a prototypical model--N-acetylphosphorylserine methylamide--revealed several factors governing the elimination of neutral phosphoryl groups through charge- and radical-induced mechanisms.
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