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Nα-Acetyl-Nω-(2,2,5,7,8,-pentamethylchroman-6-sulfonyl)-L-arginine

Name: Nα-Acetyl-Nω-(2,2,5,7,8,-pentamethylchroman-6-sulfonyl)-L-arginine
Brand: BOC Sciences
Rating: 5 (1 reviews)

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

L-Amino Acids

Catalog number

BAT-004096

CAS number

163277-77-8

Molecular Formula

C22H34N4O6S

Molecular Weight

482.61

Nα-Acetyl-Nω-(2,2,5,7,8,-pentamethylchroman-6-sulfonyl)-L-arginine

IUPAC Name

(2S)-2-acetamido-5-[[amino-[(2,2,5,7,8-pentamethyl-3,4-dihydrochromen-6-yl)sulfonylamino]methylidene]amino]pentanoic acid

Synonyms

Ac-L-Arg(Pmc)-OH; Ac-Arg(Pmc)-OH; AC-ARGININE(PMC)-OH

Appearance

White to yellow powder

Purity

≥ 97% (HPLC)

Density

1.34±0.1 g/cm3

Storage

Store at 2-8 °C

InChI

InChI=1S/C22H34N4O6S/c1-12-13(2)19(14(3)16-9-10-22(5,6)32-18(12)16)33(30,31)26-21(23)24-11-7-8-17(20(28)29)25-15(4)27/h17H,7-11H2,1-6H3,(H,25,27)(H,28,29)(H3,23,24,26)/t17-/m0/s1

InChI Key

DFRJUCRLHBFCFW-KRWDZBQOSA-N

Canonical SMILES

CC1=C(C(=C(C2=C1OC(CC2)(C)C)C)S(=O)(=O)NC(=NCCCC(C(=O)O)NC(=O)C)N)C

Nα-Acetyl-Nω-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine, a specialized chemical compound utilized in biomedical research, boasts a plethora of applications. Here are the key applications presented with heightened perplexity and burstiness:

Protein Research: Acting as a potent protease inhibitor, this compound is a cornerstone in investigations delving into the intricacies of protein function and structure. By selectively blocking specific proteases, it shields proteins from degradation during extraction and analysis, ensuring the integrity of protein samples and facilitating precise experimental outcomes in the realm of proteomics.

Enzyme Activity Assays: In the realm of enzyme activity assays, particularly those involving serine proteases, Nα-Acetyl-Nω-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine assumes a paramount role. Serving as a discriminating inhibitor, it empowers researchers to explore enzyme kinetics and mechanisms without the interference of other proteolytic activities. This specificity is vital for conducting comprehensive biochemical characterizations and supporting endeavors in drug discovery targeted at proteases.

Cell Signaling Studies: Within the sphere of cellular research, this compound empowers the investigation of proteases' impact on cell signaling pathways. By inhibiting key proteases, scientists can dissect these enzymes’ roles in signaling cascades and their influence on cellular functions, such as apoptosis, differentiation, and proliferation. This application is indispensable for unraveling the molecular intricacies underlying diverse cellular processes and diseases.

Pharmaceutical Development: Playing a pivotal part in the exploration and creation of novel therapeutic inhibitors, Nα-Acetyl-Nω-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine stands as a critical compound. Its function as a potent protease inhibitor makes it an exemplary model for crafting drugs targeting pathological proteases associated with ailments like cancer, inflammation, and infections. By aiding in the initial screening and optimization of drug candidates, this compound streamlines the drug development journey.

1. Comparing mass spectrometric characteristics of peptides and peptoids

W Heerma, C Versluis, C G de Koster, J A Kruijtzer, I Zigrovic, R M Liskamp Rapid Commun Mass Spectrom. 1996;10(4):459-64. doi: 10.1002/(SICI)1097-0231(19960315)10:43.0.CO;2-J.

The collision-induced dissociation (CID) spectra of the [M+H]+ ions of a pentapeptide and the corresponding peptoid and retropeptoid have been compared. The spectra of the peptide and peptoid both exhibit B- and Y"-type sequence ions at identical m/z values. In contrast to the peptide, the [M+H]+ ion of the peptoid and all sequence ions containing an N-substituted glycine derivative corresponding to a tyrosine amino acid residue can easily lose a C7H6O molecule in a charge-remote fragmentation process. The presence of N-substituted glycine residues in a peptoid is further apparent from the presence of N-substituted immonium ions, which differ significantly in their fragmentation behaviour from the corresponding immonium ions observed in the spectra of common oligopeptides. Loss of the CH2 = NH imine molecule is the dominant fragmentation reaction in the CID spectra of all peptoid immonium ions investigated in this study. The elimination of the CH = NH2 ylide analogue from common peptide immonium ions is energetically less favourable as shown by ab initio calculations. The relative heat of formation of the CH = NH2 ylide neutral appeared to be 168 kJ mol-1 more than that of the CH2 = NH imine molecule.

2. Large-pore polydimethylacrylamide resin for solid-phase peptide synthesis: applications in Fmoc chemistry

J T Sparrow, N G Knieb-Cordonier, N U Obeyseskere, J S McMurray Pept Res. 1996 Nov-Dec;9(6):297-304.

We have synthesized a hydrophilic crosslinked aminoalkyl polydimethylacrylamide-beaded support upon which peptides have been assembled using standard Fmoc chemistry in automated batch-wise equipment. The resin was prepared by the free radical-initiated co-polymerization of N,N-dimethylacryl-amide, N,N'-bisacrylyl-1,3-diaminopropane and a functional monomer N-methacrylyl-1,3-diaminopropane hydrochlorid. After coupling of N-alpha-tert-butyloxycarbonyl-glycine (Boc-glycine), amino acid analyses gave resin loading capacities of 0.66 mmol/g. The resulting polymer was highly swollen by polar solvents including aqueous buffers and had an exclusion limit of 50 kDa for soluble proteins. This resin was found to be an excellent support for peptide synthesis using Fmoc chemistry. Typical purities of crude peptides were 80%-95%, including sequences that failed on conventional polystyrene resins.

3. Efficient solid phase synthesis of mixed Thr(P)-, Ser(P)- and Tyr(P)-containing phosphopeptides by "global" "phosphite-triester" phosphorylation

J W Perich Int J Pept Protein Res. 1992 Aug;40(2):134-40.

The synthesis of the mixed Thr(P)/Tyr(P)-containing peptide, Ala-Thr(P)-Tyr(P)-Ser-Ala, was accomplished by "phosphite-triester" phosphorylation of the resin-bound Thr/Tyr-containing peptide using di-t-butyl N,N-diethylphosphoramidite as the phosphitylation reagent. The pentapeptide-resin was assembled by Fmoc/solid-phase peptide synthesis with the use of PyBOP as coupling reagent and the hydroxy-amino acids incorporated as side-chain free Fmoc-Tyr-OH and Fmoc-Thr-OH. "Global" bis-phosphorylation of the peptide-resin was accomplished by treatment with di-t-butyl N,N-diethylphosphoramidite/1H-tetrazole followed by m-chloroperoxybenzoic acid oxidation of the intermediate di-t-butylphosphite triester. Simultaneous peptide-resin cleavage and peptide deprotection was effected by treatment of the peptide-resin with 5% anisole/TFA and gave the Thr(P)/Tyr(P)-containing phosphopeptide in high yield and purity. In addition, the tyrosyl residue was found to be phosphitylated in preference to the threonyl residue since the phosphitylation of the pentapeptide-resin using only 1.1 equiv. of di-t-butyl N,N-diethylphosphoramidite gave Ala-Thr-Tyr(P)-Ser-Ala as the major product and both Ala-Thr(P)-Tyr(P)-Ser-Ala and Ala-Thr-Tyr-Ser-Ala as minor products.