Nα-Fmoc-Nω-(2,2,4,6,7-pentamethyl-dihydrobenzofuran-5-sulfonyl)-D-arginine
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Nα-Fmoc-Nω-(2,2,4,6,7-pentamethyl-dihydrobenzofuran-5-sulfonyl)-D-arginine

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Category
Fmoc-Amino Acids
Catalog number
BAT-003707
CAS number
187618-60-6
Molecular Formula
C34H40N4O7S
Molecular Weight
648.77
Nα-Fmoc-Nω-(2,2,4,6,7-pentamethyl-dihydrobenzofuran-5-sulfonyl)-D-arginine
IUPAC Name
(2R)-5-[[amino-[(2,2,4,6,7-pentamethyl-3H-1-benzofuran-5-yl)sulfonylamino]methylidene]amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)pentanoic acid
Synonyms
Fmoc-D-Arg(Pbf)-OH; (R)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-5-(3-((2,2,4,6,7-pentamethyl-2,3-dihydrobenzofuran-5-yl)sulfonyl)guanidino)pentanoic acid
Appearance
White powder
Purity
≥ 99.5% (Chiral purity)
Density
1.37±0.1 g/cm3(Predicted)
Melting Point
94 to 98°C
Storage
Store at 2-8°C
InChI
InChI=1S/C34H40N4O7S/c1-19-20(2)30(21(3)26-17-34(4,5)45-29(19)26)46(42,43)38-32(35)36-16-10-15-28(31(39)40)37-33(41)44-18-27-24-13-8-6-11-22(24)23-12-7-9-14-25(23)27/h6-9,11-14,27-28H,10,15-18H2,1-5H3,(H,37,41)(H,39,40)(H3,35,36,38)/t28-/m1/s1
InChI Key
HNICLNKVURBTKV-MUUNZHRXSA-N
Canonical SMILES
CC1=C2C(=C(C(=C1C)S(=O)(=O)NC(=NCCCC(C(=O)O)NC(=O)OCC3C4=CC=CC=C4C5=CC=CC=C35)N)C)CC(O2)(C)C

Nα-Fmoc-Nω-(2,2,4,6,7-pentamethyl-dihydrobenzofuran-5-sulfonyl)-D-arginine, a protected arginine derivative commonly utilized in peptide synthesis and chemical biology, finds diverse applications. Here are four key uses presented with high perplexity and burstiness:

Peptide Synthesis: Serving as a fundamental component in solid-phase peptide synthesis (SPPS), this arginine derivative plays a crucial role. The Fmoc group shields the amino terminus, guarding against undesired reactions during sequence elongation. This protective mechanism enables the precise and efficient construction of intricate peptides, minimizing side reactions to achieve optimal synthesis outcomes.

Proteomics: In the realm of proteomic exploration, Nα-Fmoc-Nω-(2,2,4,6,7-pentamethyl-dihydrobenzofuran-5-sulfonyl)-D-arginine emerges as a versatile tool for generating peptide libraries for high-throughput screening purposes. By incorporating this protected arginine into peptides, researchers delve into protein interactions, unraveling functional motifs and deciphering intricate protein functions at the molecular level. This aids in unraveling the intricacies of protein systems and their roles within biological processes.

Drug Development: A valuable asset in the realm of drug discovery, this compound facilitates the design and synthesis of peptide-based therapeutics. The selectively removable protected arginine moiety allows for targeted modifications within peptide sequences, paving the way for the creation of drug candidates with enhanced stability, efficacy, and reduced immunogenicity. This innovative approach opens avenues for developing more effective and safer pharmaceutical compounds.

Chemical Biology: Functioning as a key player in chemical biology studies, Nα-Fmoc-Nω-(2,2,4,6,7-pentamethyl-dihydrobenzofuran-5-sulfonyl)-D-arginine enables researchers to explore the role of arginine in biological systems. By integrating this derivative into peptides and proteins, scientists delve into arginine-rich motifs, unraveling their involvement in molecular recognition processes. This investigative approach sheds light on the fundamental functions of arginine in cellular mechanisms and signaling pathways, enriching our understanding of biological phenomena.

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.
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