145038-53-5

Usage

Uses

Used in Pharmaceutical Research and Development:
Fmoc-L-Aspartic acid 4-methyl ester is used as a research intermediate for the solid-phase synthesis of peptides. Its application is particularly relevant in the development of selective caspase-3 peptide inhibitors, which play a crucial role in the regulation of apoptosis and have potential therapeutic implications in various diseases, including cancer and neurodegenerative disorders.
Used in Peptide Synthesis:
In the field of peptide synthesis, Fmoc-L-Aspartic acid 4-methyl ester is utilized as a key component for the assembly of complex peptide structures. The Fmoc protecting group ensures selective protection of the amino group during the synthesis process, allowing for the stepwise addition of other amino acid residues to form the desired peptide sequence.
Used in Drug Design:
Fmoc-L-Aspartic acid 4-methyl ester is also employed in drug design, where it can be incorporated into peptide-based drug candidates. Its unique structural features enable the development of molecules with specific biological activities, such as modulating enzyme activity, targeting receptor interactions, or acting as inhibitors or agonists for various biological targets.

InChI:InChI=1/C20H19NO6/c1-26-18(22)10-17(19(23)24)21-20(25)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,21,25)(H,23,24)/t17-/m0/s1

Upstream product

• 144120-53-6 (S)-3-(((9H-fluoren-9-yl)methoxy)carbonylamino)-4-(allyloxy)-4-oxobutanoic acid 
• 858034-72-7 1-(tert-butyl) 4-methyl (((9H-fluoren-9-yl)methoxy)carbonyl)-L-aspartate 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 16856-13-6 (+)-β-methyl-L-aspartate hydrochloride 
• 32213-95-9 dimethyl L-aspartate hydrochloride 
• 67-56-1 methanol 
• 56-84-8 L-Aspartic acid 

Downstream Products

• 56-84-8 L-Aspartic acid 
• 596095-91-9 methyl (3S)-4-chloro-3-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-4-oxobutanoate 
• 1300019-48-0 methyl N¹-[2-[(4-chlorophenyl)carbonyl]-4-(methyloxy)phenyl]-N²-{[(9H-fluoren-9-ylmethyl)oxy]carbonyl}-L-α-asparaginate 
• 1300019-40-2 methyl 2-((4S)-6-(4-chlorophenyl)-8-methoxy-1-methyl-4H-benzol[f][1,2,4]triazolo[4,3-a][1,4]diazepin-4-yl)acetate 
• 1300019-43-5 (S)-methyl 2-(5-(4-chlorophenyl)-7-methoxy-2-thioxo-2,3-dihydro-1H-benzo[e][1,4]diazepin-3-yl)acetate 
• 1300019-41-3 methyl [(3S)-2-[(1Z)-2-acetylhydrazino]-5-(4-chlorophenyl)-7-(methyloxy)-3H-1,4-benzodiazepin-3-yl]acetate 
• 1300019-46-8 (S)-methyl 2-(5-(4-chlorophenyl)-7-methoxy-2-oxo-2,3-dihydro-1H-benzo[e][1,4]diazepin-3-yl)acetate 

Relevant academic research and scientific papers

Controlled Inhibition of Apoptosis by Photoactivatable Caspase Inhibitors

Caspases control regulated cell death (apoptosis), a process that is crucial in the development of multicellular organisms as well as in various diseases. In order to spatiotemporally study apoptosis, we here develop photoactivatable caspase inhibitors. These are based on cysteine-reactive acyloxymethyl ketone electrophiles connected to a peptide targeting caspases. Importantly, the aspartate crucial for recognition by caspases is caged with a photoprotecting group. Ester photocages were found to be labile, and it was critical to have a nitroindoline cage, which forms a stable amide bond with the aspartate side chain. The nitroindoline-protected inhibitors lead to an efficient turn-on of inhibitory activity after irradiation with light. They are applicable in live cells, where they prevent anti-FAS-induced apoptosis only upon irradiation. Overall, these reagents will allow a better understanding of the spatial and temporal dimensions of apoptosis in complex, dynamic systems.Activation of caspases leads to apoptosis. Chakrabarty and Verhelst designed, synthesized, and evaluated photocaged caspase inhibitors that allow caspase inhibition only upon irradiation with light. These reagents allow for a precise spatial and temporal control over caspase inhibition and may be used to study apoptosis in space and time.

PROCESSES FOR PREPARING AMINO-SUBSTITUTED GAMMA-LACTAMS

The present application describes general process for the preparation of amino-substitued gamma-lactams involving the reaction of synthons of the general Formulae (I) and (VI): with amines. The processes are amenable to solid phase synthetic techniques and therefore allow the efficient incorporation of amino-substitued gamma-lactams into a wide variety of structural scaffolds, including, in particular peptides.

Positional scanning for peptide secondary structure by systematic solid-phase synthesis of amino lactam peptides

Incorporation of amino lactams into biologically active peptides has been commonly used to restrict conformational mobility, enhance selectivity, and increase potency. A solid-phase method using a Fmoc-protection strategy has been developed for the systematic synthesis of peptides containing configurationally defined α- and β-amino γ-lactams. N-Alkylation of N-silyl peptides with five- and six-member cyclic sulfamidates 9 and 8 minimized bis-alkylation and provided N-alkyl peptides,which underwent lactam annulation under microwave heating. Employing th is solid-phase protocol on the growth hormone secretagogue GHRP-6, as well as on the allosteric modulator of the IL-1 receptor 101.10, has furnished 16 lactam derivatives and validated the effectiveness of this approach on peptides bearing aliphatic, aromatic, branched, charged, and heteroatomic side chains. The binding affinity IC 50 values of the GHRP-6 lactam analogues on both the GHS-R1a and CD36 receptors are reported as well as inhibition of thymocyte proliferation measurements for the 101.10 lactam analogues. In these cases, lactam analogues were prepared exhibiting similar or improved properties compared with the parent peptide. Considering the potential for amino lactams to induce peptide turn conformations, the effective method described herein for their supported construction on growing peptides, and for the systematical amino lactam scan of peptides, has proven useful for the rapid identification of the secondary structure necessary for peptide biological activity.

Pd-C-induced catalytic transfer hydrogenation with triethylsilane

(Chemical Equation Presented) In situ generation of molecular hydrogen by addition of triethylsilane to palladium-charcoal catalyst results in rapid and efficient reduction of multiple bonds, azides, imines, and nitro groups, as well as benzyl group and allyl group deprotection under mild, neutral conditions.