Fmoc-S-methyl-L-cysteine
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Fmoc-S-methyl-L-cysteine

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Category
Fmoc-Amino Acids
Catalog number
BAT-003833
CAS number
138021-87-1
Molecular Formula
C19H19NO4S
Molecular Weight
357.43
Fmoc-S-methyl-L-cysteine
IUPAC Name
(2R)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-methylsulfanylpropanoic acid
Synonyms
Fmoc-L-Cys(Me)-OH; (2R)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-methylsulfanylpropanoic acid
Appearance
White powder
Purity
≥ 98% (HPLC)
Density
1.308±0.06 g/cm3
Melting Point
142-146 °C
Boiling Point
594.5±50.0 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C19H19NO4S/c1-25-11-17(18(21)22)20-19(23)24-10-16-14-8-4-2-6-12(14)13-7-3-5-9-15(13)16/h2-9,16-17H,10-11H2,1H3,(H,20,23)(H,21,22)/t17-/m0/s1
InChI Key
SKNJDZVHMNQAGO-KRWDZBQOSA-N
Canonical SMILES
CSCC(C(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13

Fmoc-S-methyl-L-cysteine, a derivative of cysteine crucial in peptide synthesis and biochemical research, has diverse applications.

Peptide Synthesis: Widely employed in peptide synthesis as a protected form of cysteine, Fmoc-S-methyl-L-cysteine plays a pivotal role in ensuring the purity and accurate assembly of peptide chains. The Fmoc group shields the amine group throughout synthesis, enabling selective deprotection and coupling reactions. This derivative is indispensable for the development of therapeutic peptides and the study of protein structures.

Protein Engineering: In the realm of protein engineering, Fmoc-S-methyl-L-cysteine is utilized to introduce modified cysteine residues into proteins, offering insights into protein folding, stability, and function. Additionally, incorporating this derivative facilitates the attachment of probes or labels, aiding in various biochemical assays and imaging techniques. This versatile application enhances the precision of protein studies.

Drug Design: A key player in drug design and development, Fmoc-S-methyl-L-cysteine is particularly valuable for creating peptidomimetics, which often require non-natural amino acid derivatives to enhance stability and bioavailability. This derivative enables the introduction of structural variations in peptides to optimize their therapeutic properties, propelling advancements in drug development and design.

Biochemical Research: Essential for studying post-translational modifications and protein-protein interactions, Fmoc-S-methyl-L-cysteine is a cornerstone in biochemical research. By incorporating this derivative into experimental systems, scientists can delve into the effects of specific modifications on protein behavior, leading to novel insights into cellular processes and the development of cutting-edge biochemical tools. This application broadens the horizons of biochemical research.

1.A 'conovenomic' analysis of the milked venom from the mollusk-hunting cone snail Conus textile--the pharmacological importance of post-translational modifications.
Bergeron ZL1, Chun JB, Baker MR, Sandall DW, Peigneur S, Yu PY, Thapa P, Milisen JW, Tytgat J, Livett BG, Bingham JP. Peptides. 2013 Nov;49:145-58. doi: 10.1016/j.peptides.2013.09.004. Epub 2013 Sep 18.
Cone snail venoms provide a largely untapped source of novel peptide drug leads. To enhance the discovery phase, a detailed comparative proteomic analysis was undertaken on milked venom from the mollusk-hunting cone snail, Conus textile, from three different geographic locations (Hawai'i, American Samoa and Australia's Great Barrier Reef). A novel milked venom conopeptide rich in post-translational modifications was discovered, characterized and named α-conotoxin TxIC. We assign this conopeptide to the 4/7 α-conotoxin family based on the peptide's sequence homology and cDNA pre-propeptide alignment. Pharmacologically, α-conotoxin TxIC demonstrates minimal activity on human acetylcholine receptor models (100 μM, <5% inhibition), compared to its high paralytic potency in invertebrates, PD50 = 34.2 nMol kg(-1). The non-post-translationally modified form, [Pro](2,8)[Glu](16)α-conotoxin TxIC, demonstrates differential selectivity for the α3β2 isoform of the nicotinic acetylcholine receptor with maximal inhibition of 96% and an observed IC50 of 5.
2.Chemical synthesis and receptor binding of catfish somatostatin: a disulfide-bridged beta-D-Galp-(1-->3)-alpha-D-GalpNAc O-glycopeptide.
Chen L1, Jensen KJ, Tejbrant J, Taylor JE, Morgan BA, Barany G. J Pept Res. 2000 Jan;55(1):81-91.
The glycopeptide hormone catfish somatostatin (somatostatin-22) has the amino acid sequence H-Asp-Asn-Thr-Val-Thr-Ser-Lys-Pro-Leu-Asn-Cys-Met-Asn-Tyr-Phe-Trp-Lys-Se r-Arg-Thr-Ala-Cys-OH; it includes a cyclic disulfide connecting the two Cys residues, and the major naturally occurring glycoform contains D-GalNAc and D-Gal O-glycosidically linked to Thr5. The linear sequence was assembled smoothly starting with an Fmoc-Cys(Trt)-PAC-PEG-PS support, using stepwise Fmoc solid-phase chemistry. In addition to the nonglycosylated peptide, two glycosylated forms of somatostatin-22 were accessed by incorporating as building blocks, respectively, Nalpha-Fmoc-Thr(Ac3-alpha-D-GalNAc)-OH and Nalpha-Fmoc-Thr(Ac4-beta-D-Gal-(1-->3)-Ac2-alpha-D-GalNAc)-O H. Acidolytic deprotection/cleavage of these peptidyl-resins with trifluoroacetic acid/scavenger cocktails gave the corresponding acetyl-protected glycopeptides with free sulfhydryl functions. Deacetylation, by methanolysis in the presence of catalytic sodium methoxide, was followed by mild oxidation at pH 7, mediated by Nalpha-dithiasuccinoyl (Dts)-glycine, to provide the desired monomeric cyclic disulfides.
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