N-α-(t-Butoxycarbonyl)-S-octyl-L-cysteine
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N-α-(t-Butoxycarbonyl)-S-octyl-L-cysteine

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Category
BOC-Amino Acids
Catalog number
BAT-003172
CAS number
67194-12-1
Molecular Formula
C16H31NO4S
Molecular Weight
333.49
N-α-(t-Butoxycarbonyl)-S-octyl-L-cysteine
IUPAC Name
(2R)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-3-octylsulfanylpropanoic acid
Synonyms
Boc-Cys(Octyl)-OH; Boc-Cys{(CH2)7-CH3}-OH
Purity
95%
InChI
InChI=1S/C16H31NO4S/c1-5-6-7-8-9-10-11-22-12-13(14(18)19)17-15(20)21-16(2,3)4/h13H,5-12H2,1-4H3,(H,17,20)(H,18,19)/t13-/m0/s1
InChI Key
KUBMJZUXYLPQFI-ZDUSSCGKSA-N
Canonical SMILES
CCCCCCCCSCC(C(=O)O)NC(=O)OC(C)(C)C

N-α-(t-Butoxycarbonyl)-S-octyl-L-cysteine is a chemical compound with a range of specialized applications in the field of chemistry and biosciences. Here are some key applications of N-α-(t-Butoxycarbonyl)-S-octyl-L-cysteine:

Peptide Synthesis: N-α-(t-Butoxycarbonyl)-S-octyl-L-cysteine is extensively used in peptide synthesis as a protected amino acid. Its presence helps to prevent unwanted side reactions during the formation of peptide bonds. This application ensures the accurate and efficient synthesis of complex peptides for research and therapeutic purposes.

Drug Development: This compound is utilized in the early stages of drug development to create model compounds and analogs. By incorporating N-α-(t-Butoxycarbonyl)-S-octyl-L-cysteine into drug candidates, researchers can modify and study their pharmacokinetic and pharmacodynamic properties. This can lead to the discovery of new drugs with improved efficacy and safety profiles.

Protein Engineering: N-α-(t-Butoxycarbonyl)-S-octyl-L-cysteine serves as a valuable tool in protein engineering, where it is used to introduce specific modifications into proteins. These modifications can alter protein stability, activity, or solubility, providing insights into protein function and enabling the creation of proteins with desirable characteristics. This application is essential in the design of novel biocatalysts and therapeutic proteins.

Analytical Chemistry: In analytical chemistry, N-α-(t-Butoxycarbonyl)-S-octyl-L-cysteine is employed as a reagent for the detection and quantification of thiol groups in various samples. By reacting with thiols, it forms stable derivatives that can be easily analyzed using techniques such as chromatography and mass spectrometry. This is crucial for studying biological samples and monitoring chemical reactions.

1. Substrate recognition by oligosaccharyltransferase. Studies on glycosylation of modified Asn-X-Thr/Ser tripeptides
J K Welply, P Shenbagamurthi, W J Lennarz, F Naider J Biol Chem. 1983 Oct 10;258(19):11856-63.
The minimum primary structural requirement for N-glycosylation of proteins is the sequence -Asn-X-Thr/Ser-. In the present study, NH2-terminal derivatives of Asn-Leu-Thr-NH2 and peptides with asparagine replacements have been tested as substrates or inhibitors of N-glycosylation. The glycosylation of a known acceptor, N alpha-[3H]Ac-Asn-Leu-Thr-NHCH3, was optimized in chicken oviduct microsomes. The reaction was shown to be dependent upon Mn2+ and linear for 10 min at 30 degrees C; the apparent Km for the peptide was found to be 10 microM. N alpha-Acyl derivatives of Asn-Leu-Thr-NH2 (N-acetyl, N-benzoyl, N-octanoyl, or N-t-butoxycarbonyl) inhibited the glycosylation of N alpha-[3H] Ac-Asn-Leu-Thr-NHCH3 in a dose-dependent manner; additional experiments demonstrated that these compounds were alternative substrates rather than true inhibitors. The benzoyl and octanoyl derivatives were 10 times as effective as N alpha-Ac-Asn-Leu-Thr-NH2 in inhibiting glycosylation. In contrast, peptides containing asparagine modifications or substitutions were neither substrates nor inhibitors of N-glycosylation. They did not compete for glycosylation of 3H-peptide at 100-fold greater concentrations, and did not deplete endogenous pools of oligosaccharide-lipid. Thus, the asparagine side chain is an absolute requirement for recognition by the transferase. The majority of the glycosylated product (61%), but only 1% of the unglycosylated peptide, remained associated with the microsomes after high speed centrifugation. A large 41-amino acid residue acceptor peptide, alpha-lac17-58, was a poor substitute for glycosylation unless detergent was added to the microsomes. In contrast, glycosylation of tripeptide acceptors was not stimulated by detergent. Both of these findings suggest that the tripeptides are freely permeable to the microsomal membrane and support the earlier conclusion that glycosylation of proteins occurs at the luminal face of the microsomes.
2. Enantioselective immunorecognition of protein modification with optically active ibuprofen using polyclonal antibody
Hiromi Ito, Shunji Ishiwata, Takeshi Kosaka, Rika Nakashima, Harunori Takeshita, Sakiko Negoro, Masako Maeda, Shigeo Ikegawa J Chromatogr B Analyt Technol Biomed Life Sci. 2004 Jun 25;806(1):11-7. doi: 10.1016/j.jchromb.2004.01.040.
Formation of covalently bound protein adducts with 2-arylpropionic acids (2-APAs) has been proposed as a possible explanation for hypersensitivity and toxic responses to chiral carboxylic acid drugs. To identify the cellular proteins chemically modified with optically active (S)-ibuprofen, we generate polyclonal antibodies by immunizing rabbits with immunogen coupled to bovine serum albumin (BSA) via the spacer of 4-aminobutyric acid. The resulting antibodies largely cross-reacted with N-alpha-(t-butoxycarbonyl)--(S)-ibuprofenyl lysine as well as with the conjuguated (S)-ibuprofen with glycine and taurine and unconjugated (S)-ibuprofen, enabling enantioselective detection of (S)-ibuprofen residues anchored on ovalbumin molecules, introduced by the reaction of the ibuprofen p-nitrophenyl ester. Furthermore, immunoblotting with an antibody allows the enantioselective detection of (S)-ibuprofen-introduced glutathione-S-transferase (GST). These results indicate that the developed method will be useful for monitoring the generation and localization of protein covalently bound with (S)-ibuprofen, which may be the cause of ibuprofen-induced toxicity.
3. Evaluating Fmoc-amino acids as selective inhibitors of butyrylcholinesterase
Jeannette Gonzalez, Jennifer Ramirez, Jason P Schwans Amino Acids. 2016 Dec;48(12):2755-2763. doi: 10.1007/s00726-016-2310-4. Epub 2016 Aug 13.
Cholinesterases are involved in neuronal signal transduction, and perturbation of function has been implicated in diseases, such as Alzheimer's and Huntington's disease. For the two major classes of cholinesterases, such as acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), previous studies reported BChE activity is elevated in patients with Alzheimer's disease, while AChE levels remain the same or decrease. Thus, the development of potent and specific inhibitors of BChE have received much attention as a potential therapeutic in the alleviation of neurodegenerative diseases. In this study, we evaluated amino acid analogs as selective inhibitors of BChE. Amino acid analogs bearing a 9-fluorenylmethyloxycarbonyl (Fmoc) group were tested, as the Fmoc group has structural resemblance to previously described inhibitors. We identified leucine, lysine, and tryptophan analogs bearing the Fmoc group as selective inhibitors of BChE. The Fmoc group contributed to inhibition, as analogs bearing a carboxybenzyl group showed ~tenfold higher values for the inhibition constant (K I value). Inclusion of a t-butoxycarbonyl on the side chain of Fmoc tryptophan led to an eightfold lower K I value compared to Fmoc tryptophan alone suggesting that modifications of the amino acid side chains may be designed to create inhibitors with higher affinity. Our results identify Fmoc-amino acids as a scaffold upon which to design BChE-specific inhibitors and provide the foundation for further experimental and computational studies to dissect the interactions that contribute to inhibitor binding.
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