Fmoc-L-Asn(Me)-OH
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Fmoc-L-Asn(Me)-OH

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Category
Fmoc-Amino Acids
Catalog number
BAT-008721
CAS number
149204-93-3
Molecular Formula
C20H20N2O5
Molecular Weight
368.4
IUPAC Name
(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-(methylamino)-4-oxobutanoic acid
Synonyms
N-Fmoc-N'-methyl-L-asparagine
InChI
InChI=1S/C20H20N2O5/c1-21-18(23)10-17(19(24)25)22-20(26)27-11-16-14-8-4-2-6-12(14)13-7-3-5-9-15(13)16/h2-9,16-17H,10-11H2,1H3,(H,21,23)(H,22,26)(H,24,25)/t17-/m0/s1
InChI Key
GCQNMZCRYMMHTM-KRWDZBQOSA-N
Canonical SMILES
CNC(=O)CC(C(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13

Fmoc-L-Asn(Me)-OH, a derivative of modified amino acid, plays a crucial role in peptide synthesis and research. Here are four key applications of Fmoc-L-Asn(Me)-OH, presented with high perplexity and burstiness:

Synthetic Peptide Production: Serving as a foundational element in solid-phase peptide synthesis (SPPS), Fmoc-L-Asn(Me)-OH facilitates the incorporation of methylated asparagine residues into peptide chains. This modification enhances the stability and enzymatic resistance of peptides, enabling researchers to explore protein interactions and craft therapeutic agents with precision.

Protein Engineering: By integrating Fmoc-L-Asn(Me)-OH into proteins, scientists can manipulate their properties for diverse applications. This modified amino acid serves as a tool for investigating the effects of methylation on protein function and structural integrity. Its application in protein engineering aids in unraveling the complexities of post-translational modifications and their implications on protein behavior, opening new avenues for research.

Drug Discovery: In the realm of drug development, Fmoc-L-Asn(Me)-OH plays a vital role in synthesizing peptide-based drug candidates. Methylated peptides synthesized using this compound often exhibit enhanced pharmacokinetic properties such as improved bioavailability and stability. Leveraging Fmoc-L-Asn(Me)-OH, researchers can design and refine peptides with heightened therapeutic efficacy, advancing the field of drug discovery with innovative solutions.

Biomolecular Research: Within the domain of molecular biology, Fmoc-L-Asn(Me)-OH is instrumental in creating specific peptide sequences for research endeavors. These methylated peptides function as substrates or inhibitors in enzymatic studies, aiding in the exploration of enzyme mechanisms and substrate specificity. This application is essential for unraveling intricate biochemical pathways, advancing our understanding of biomolecular interactions, and facilitating the development of targeted enzyme inhibitors for therapeutic purposes.

1. Low-Dimensional Architectures in Isomeric cis-PtCl2{Ph2PCH2N(Ar)CH2PPh2} Complexes Using Regioselective-N(Aryl)-Group Manipulation
Peter De'Ath, Mark R J Elsegood, Noelia M Sanchez-Ballester, Martin B Smith Molecules. 2021 Nov 11;26(22):6809. doi: 10.3390/molecules26226809.
The solid-state behaviour of two series of isomeric, phenol-substituted, aminomethylphosphines, as the free ligands and bound to PtII, have been extensively studied using single crystal X-ray crystallography. In the first library, isomeric diphosphines of the type Ph2PCH2N(Ar)CH2PPh2 [1a-e; Ar = C6H3(Me)(OH)] and, in the second library, amide-functionalised, isomeric ligands Ph2PCH2N{CH2C(O)NH(Ar)}CH2PPh2 [2a-e; Ar = C6H3(Me)(OH)], were synthesised by reaction of Ph2PCH2OH and the appropriate amine in CH3OH, and isolated as colourless solids or oils in good yield. The non-methyl, substituted diphosphines Ph2PCH2N{CH2C(O)NH(Ar)}CH2PPh2 [2f, Ar = 3-C6H4(OH); 2g, Ar = 4-C6H4(OH)] and Ph2PCH2N(Ar)CH2PPh2 [3, Ar = 3-C6H4(OH)] were also prepared for comparative purposes. Reactions of 1a-e, 2a-g, or 3 with PtCl2(η4-cod) afforded the corresponding square-planar complexes 4a-e, 5a-g, and 6 in good to high isolated yields. All new compounds were characterised using a range of spectroscopic (1H, 31P{1H}, FT-IR) and analytical techniques. Single crystal X-ray structures have been determined for 1a, 1b∙CH3OH, 2f∙CH3OH, 2g, 3, 4b∙(CH3)2SO, 4c∙CHCl3, 4d∙½Et2O, 4e∙½CHCl3∙½CH3OH, 5a∙½Et2O, 5b, 5c∙¼H2O, 5d∙Et2O, and 6∙(CH3)2SO. The free phenolic group in 1b∙CH3OH, 2f∙CH3OH,2g, 4b∙(CH3)2SO, 5a∙½Et2O, 5c∙¼H2O, and 6∙(CH3)2SO exhibits various intra- or intermolecular O-H∙∙∙X (X = O, N, P, Cl) hydrogen contacts leading to different packing arrangements.
3. Modeling tyrosinase and catecholase activity using new m-Xylyl-based ligands with bidentate alkylamine terminal coordination
Sukanta Mandal, Jhumpa Mukherjee, Francesc Lloret, Rabindranath Mukherjee Inorg Chem. 2012 Dec 17;51(24):13148-61. doi: 10.1021/ic3013848. Epub 2012 Nov 29.
Chemical model systems possessing the reactivity aspects of both tyrosinase and catechol oxidase are presented. Using two m-xylyl-based ligands providing bidentate alkylamine terminal coordination, 1,3-bis[(N,N-dimethylaminoethyl)aminomethyl]benzene (L(H,H)) and 1,3-bis[(N,N,N'-trimethylaminoethyl)aminomethyl]benzene (L(Me,Me)), four new dicopper(I) complexes, [Cu(I)(2)(L(H,H))(MeCN)(4)][ClO(4)](2) (1), [Cu(I)(2)(L(H,H))(PPh(3))(2)(MeCN)(2)][ClO(4)](2) (2), [Cu(I)(2)(L(Me,Me))(MeCN)(2)][ClO(4)](2) (3), and [Cu(I)(2)(L(Me,Me))(PPh(3))(2)][ClO(4)](2) (4), have been synthesized and characterized. Complex 2 has been structurally characterized. Reaction of the dicopper(I) complex 3(2+) with dioxygen at 183 K generates putative bis(μ-oxo)dicopper(III) intermediate (absorption spectroscopy). Oxygenation of 1 and 3 brings about m-xylyl-ring hydroxylation (monooxygenase-like activity), with a noticeable color change from pale-yellow to dark green. The presence of phenoxo- and hydroxo-bridges in the end products [Cu(II)(2)(L(H,H)-O)(OH)(MeCN)(2)][ClO(4)](2) (5) and [Cu(II)(2)(L(Me,Me)-O)(OH)(OClO(3))][ClO(4)]·MeCN(6) has been authenticated by structural characterization. Oxygenation of 3 afforded not only the green complex 6 isolation but also a blue complex [Cu(II)(2)(L(Me,Me))(OH)(2)][ClO(4)](2) (7). Variable temperature magnetic susceptibility measurements on 5 and 6 establish that the Cu(II) centers are strongly antiferromagnetically coupled [singlet-triplet energy gap (J) = -528 cm(-1) (5) and -505 cm(-1) (6)]. The abilities of phenoxo- and hydroxo-bridged dicopper(II) complexes 5 and 6, the previously reported complex [Cu(II)(2)(L(1)-O)(OH)(OClO(3))(2)]·1.5H(2)O (8) (L(1)-OH = 1,3-bis[(2-dimethylaminoethyl)iminomethyl]phenol), and [Cu(II)(2)(L(2)-O)(OH)(OClO(3))()][ClO(4)]() (9) (L(2)-OH = 1,3-[(2-dimethylaminoethyl)iminomethyl][(N,N,N'-trimethyl)aminoethyl]-4-methylphenol) have been examined to catalyze the oxidation of catechol to quinone (catecholase activity of tyrosinase and catechol oxidase-like activity) by employing the model substrate 3,5-di-tert-butylcatechol. Saturation kinetic studies have been performed on these systems to arrive at the following reactivity order [k(cat)/K(M) (catalytic efficiency) × 10(-3) (M(-1) h(-1))]: 470 (6) > 367 (5) > 128 (9) > 90 (8).
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