N-α-(9-Fluorenylmethoxycarbonyl)-S-octyl-L-cysteine
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N-α-(9-Fluorenylmethoxycarbonyl)-S-octyl-L-cysteine

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Category
Fmoc-Amino Acids
Catalog number
BAT-005478
CAS number
210883-65-1
Molecular Formula
C26H33NO4S
Molecular Weight
455.61
N-α-(9-Fluorenylmethoxycarbonyl)-S-octyl-L-cysteine
IUPAC Name
(2R)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-octylsulfanylpropanoic acid
Synonyms
Fmoc-Cys(Octyl)-OH; Fmoc-Cys{(CH2)7-CH3}-OH; (L)-2-(9H-fluoren-9-ylmethoxycarbonyl)-3-octylsulfanyl-propionic acid
Purity
≥ 95%
InChI
InChI=1S/C26H33NO4S/c1-2-3-4-5-6-11-16-32-18-24(25(28)29)27-26(30)31-17-23-21-14-9-7-12-19(21)20-13-8-10-15-22(20)23/h7-10,12-15,23-24H,2-6,11,16-18H2,1H3,(H,27,30)(H,28,29)/t24-/m0/s1
InChI Key
MGPYORYNCXOZLW-DEOSSOPVSA-N
Canonical SMILES
CCCCCCCCSCC(C(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13

N-α-(9-Fluorenylmethoxycarbonyl)-S-octyl-L-cysteine, a specialized compound crucial in peptide synthesis and biochemistry research, boasts a myriad of applications. Here are four key applications:

Peptide Synthesis: Acting as a prevalent protecting group for cysteine residues in solid-phase peptide synthesis, N-α-(9-Fluorenylmethoxycarbonyl)-S-octyl-L-cysteine, or Fmoc-S-octyl-L-cysteine, shields the amino group of cysteine from undesired reactions, ensuring the precise construction of peptides. This precision is paramount in drug development and biochemical research, where peptides play pivotal roles.

Protein Engineering: By strategically modifying proteins using N-α-(9-Fluorenylmethoxycarbonyl)-S-octyl-L-cysteine, researchers can introduce chemical handles for subsequent modifications, such as linking fluorescent probes or other functional molecules. This approach is critical for probing protein functions, interactions, and cellular localization, unveiling the intricate realm of protein biology.

Structure-Activity Relationship (SAR) Studies: Essential in unraveling the structure-activity relationships of peptides and proteins, this compound permits researchers to methodically alter cysteine residues with the Fmoc-S-octyl group, examining the impacts on biological activity and stability. Such investigations are pivotal for crafting potent drugs and therapeutic peptides that can revolutionize medical treatments.

Bioconjugation: By leveraging N-α-(9-Fluorenylmethoxycarbonyl)-S-octyl-L-cysteine to introduce reactive groups into peptides for bioconjugation purposes, researchers can affix various molecules like PEG, drugs, or biomolecules to peptides. This modification enhances the pharmacokinetic properties and therapeutic potential of peptide-based drugs, unveiling novel avenues for drug delivery and treatment strategies.

1. A 'conovenomic' analysis of the milked venom from the mollusk-hunting cone snail Conus textile--the pharmacological importance of post-translational modifications
Zachary L Bergeron, et al. 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 5.4 ± 0.5 μM. Interestingly its comparative PD50 (3.6 μMol kg(-1)) in invertebrates was ~100 fold more than that of the native peptide. Differentiating α-conotoxin TxIC from other α-conotoxins is the high degree of post-translational modification (44% of residues). This includes the incorporation of γ-carboxyglutamic acid, two moieties of 4-trans hydroxyproline, two disulfide bond linkages, and C-terminal amidation. These findings expand upon the known chemical diversity of α-conotoxins and illustrate a potential driver of toxin phyla-selectivity within Conus.
2. Syntheses of T(N) building blocks Nalpha-(9-fluorenylmethoxycarbonyl)-O-(3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-galactopyranosyl)-L-serine/L-threonine pentafluorophenyl esters: comparison of protocols and elucidation of side reactions
Mian Liu, Victor G Young Jr, Sachin Lohani, David Live, George Barany Carbohydr Res. 2005 May 23;340(7):1273-85. doi: 10.1016/j.carres.2005.02.029.
T(N) antigen building blocks Nalpha-(9-fluorenylmethoxycarbonyl)-O-(3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-galactopyranosyl)-L-serine/L-threonine pentafluorophenyl ester [Fmoc-L-Ser/L-Thr(Ac3-alpha-D-GalN3)-OPfp, 13/14] have been synthesized by two different routes, which have been compared. Overall isolated yields [three or four chemical steps, and minimal intermediary purification steps] of enantiopure 13 and 14 were 5-18% and 6-10%, respectively, based on 3,4,6-tri-O-acetyl-D-galactal (1). A byproduct of the initial azidonitration reaction of the synthetic sequence, that is, N-acetyl-3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-galactopyranosylamine (5), has been characterized by X-ray crystallography, and shown by 1H NMR spectroscopy to form complexes with lithium bromide, lithium iodide, or sodium iodide in acetonitrile-d3. Intermediates 3,4,6-tri-O-acetyl-2-azido-2-deoxy-alpha-D-galactopyranosyl bromide (6) and 3,4,6-tri-O-acetyl-2-azido-2-deoxy-beta-D-galactopyranosyl chloride (7) were used to glycosylate Nalpha-(9-fluorenylmethoxycarbonyl)-L-serine/L-threonine pentafluorophenyl esters [Fmoc-L-Ser/L-Thr-OPfp, 11/12]. Previously undescribed low-level dehydration side reactions were observed at this stage; the unwanted byproducts were easily removed by column chromatography.
3. Preparation of protected peptidyl thioester intermediates for native chemical ligation by Nalpha-9-fluorenylmethoxycarbonyl (Fmoc) chemistry: considerations of side-chain and backbone anchoring strategies, and compatible protection for N-terminal cysteine
C M Gross, D Lelièvre, C K Woodward, G Barany J Pept Res. 2005 Mar;65(3):395-410. doi: 10.1111/j.1399-3011.2005.00241.x.
Native chemical ligation has proven to be a powerful method for the synthesis of small proteins and the semisynthesis of larger ones. The essential synthetic intermediates, which are C-terminal peptide thioesters, cannot survive the repetitive piperidine deprotection steps of N(alpha)-9-fluorenylmethoxycarbonyl (Fmoc) chemistry. Therefore, peptide scientists who prefer to not use N(alpha)-t-butyloxycarbonyl (Boc) chemistry need to adopt more esoteric strategies and tactics in order to integrate ligation approaches with Fmoc chemistry. In the present work, side-chain and backbone anchoring strategies have been used to prepare the required suitably (partially) protected and/or activated peptide intermediates spanning the length of bovine pancreatic trypsin inhibitor (BPTI). Three separate strategies for managing the critical N-terminal cysteine residue have been developed: (i) incorporation of N(alpha)-9-fluorenylmethoxycarbonyl-S-(N-methyl-N-phenylcarbamoyl)sulfenylcysteine [Fmoc-Cys(Snm)-OH], allowing creation of an otherwise fully protected resin-bound intermediate with N-terminal free Cys; (ii) incorporation of N(alpha)-9-fluorenylmethoxycarbonyl-S-triphenylmethylcysteine [Fmoc-Cys(Trt)-OH], generating a stable Fmoc-Cys(H)-peptide upon acidolytic cleavage; and (iii) incorporation of N(alpha)-t-butyloxycarbonyl-S-fluorenylmethylcysteine [Boc-Cys(Fm)-OH], generating a stable H-Cys(Fm)-peptide upon cleavage. In separate stages of these strategies, thioesters are established at the C-termini by selective deprotection and coupling steps carried out while peptides remain bound to the supports. Pilot native chemical ligations were pursued directly on-resin, as well as in solution after cleavage/purification.
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