Boc-L-glutamic acid α-9-fluorenylmethyl ester
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Boc-L-glutamic acid α-9-fluorenylmethyl ester

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Category
BOC-Amino Acids
Catalog number
BAT-002767
CAS number
133906-29-3
Molecular Formula
C24H27NO6
Molecular Weight
425.48
Boc-L-glutamic acid α-9-fluorenylmethyl ester
IUPAC Name
(4S)-5-(9H-fluoren-9-ylmethoxy)-4-[(2-methylpropan-2-yl)oxycarbonylamino]-5-oxopentanoic acid
Synonyms
Boc-L-Glu-Ofm; N-alpha-tert-Butyloxycarbonyl-glutamic acid beta-fluorenylmethyl ester
Appearance
White powder
Purity
≥ 99% (HPLC)
Storage
Store at 2-8 °C
InChI
InChI=1S/C24H27NO6/c1-24(2,3)31-23(29)25-20(12-13-21(26)27)22(28)30-14-19-17-10-6-4-8-15(17)16-9-5-7-11-18(16)19/h4-11,19-20H,12-14H2,1-3H3,(H,25,29)(H,26,27)/t20-/m0/s1
InChI Key
KSYVYHUPZNONJS-FQEVSTJZSA-N
Canonical SMILES
CC(C)(C)OC(=O)NC(CCC(=O)O)C(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13

Boc-L-glutamic acid α-9-fluorenylmethyl ester, a versatile protected amino acid derivative with extensive applications in peptide synthesis and biochemical research, offers a plethora of possibilities.

Peptide Synthesis: Positioned as a foundational element in solid-phase peptide synthesis, this compound serves as a shielded building block for glutamic acid. The Boc group delicately protects the amino group, while the 9-fluorenylmethyl ester guards the carboxyl group throughout elongation. This meticulous protection strategy facilitates the gradual assembly of peptides, ensuring heightened purity and yield in the final products.

Bioconjugation Studies: Venturing into the realm of bioconjugation experiments, Boc-L-glutamic acid α-9-fluorenylmethyl ester plays a pivotal role in crafting glutamic acid-enriched peptides. By selectively revealing functional groups, researchers can anchor these peptides to a myriad of biomolecules or surfaces, propelling the creation of targeted delivery systems and delving into the intricate realm of protein interactions.

Structural Biology: In the intricate landscape of structural biology, this compound aids in constructing peptides that emulate protein segments rich in glutamic acid. These peptides serve as indispensable tools for scrutinizing protein structure and interactions using sophisticated methodologies like NMR spectroscopy and X-ray crystallography. Unraveling the significance of glutamic acid residues contributes to decoding the complexities of protein folding and functional roles.

Drug Discovery: At the forefront of drug discovery, scientists harness Boc-L-glutamic acid α-9-fluorenylmethyl ester to design and synthesize peptide-based drug candidates. Its integration into peptides can significantly impact properties such as solubility, stability, and bioactivity. Through meticulous adjustments in the peptide sequence, researchers can fine-tune therapeutic characteristics, laying the foundation for the development of innovative pharmaceuticals with enhanced efficacy.

1. Practical spectrophotometric assay for the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase, a potential antibiotic target
Tahirah K Heath, et al. PLoS One. 2018 Apr 26;13(4):e0196010. doi: 10.1371/journal.pone.0196010. eCollection 2018.
A new enzymatic assay for the bacterial enzyme succinyl-diaminopimelate desuccinylase (DapE, E.C. 3.5.1.18) is described. This assay employs N6-methyl-N2-succinyl-L,L-diaminopimelic acid (N6-methyl-L,L-SDAP) as the substrate with ninhydrin used to detect cleavage of the amide bond of the modified substrate, wherein N6-methylation enables selective detection of the primary amine enzymatic product. Molecular modeling supported preparation of the mono-N6-methylated-L,L-SDAP as an alternate substrate for the assay, given binding in the active site of DapE predicted to be comparable to the endogenous substrate. The alternate substrate for the assay, N6-methyl-L,L-SDAP, was synthesized from the tert-butyl ester of Boc-L-glutamic acid employing a Horner-Wadsworth-Emmons olefination followed by an enantioselective reduction employing Rh(I)(COD)(S,S)-Et-DuPHOS as the chiral catalyst. Validation of the new ninhydrin assay was demonstrated with known inhibitors of DapE from Haemophilus influenza (HiDapE) including captopril (IC50 = 3.4 [± 0.2] μM, 3-mercaptobenzoic acid (IC50 = 21.8 [±2.2] μM, phenylboronic acid (IC50 = 316 [± 23.6] μM, and 2-thiopheneboronic acid (IC50 = 111 [± 16] μM. Based on these data, this assay is simple and robust, and should be amenable to high-throughput screening, which is an important step forward as it opens the door to medicinal chemistry efforts toward the discovery of DapE inhibitors that can function as a new class of antibiotics.
2. Incorporation of Glutamic Acid or Amino-Protected Glutamic Acid into Poly(Glycerol Sebacate): Synthesis and Characterization
Yi-Sheng Jiang, Ming-Hsien Hu, Jeng-Shiung Jan, Jin-Jia Hu Polymers (Basel). 2022 May 29;14(11):2206. doi: 10.3390/polym14112206.
Poly(glycerol sebacate) (PGS), a soft, tough elastomer with excellent biocompatibility, has been exploited successfully in many tissue engineering applications. Although tunable to some extent, the rapid in vivo degradation kinetics of PGS is not compatible with the healing rate of some tissues. The incorporation of L-glutamic acid into a PGS network with an aim to retard the degradation rate of PGS through the formation of peptide bonds was conducted in this study. A series of poly(glycerol sebacate glutamate) (PGSE) containing various molar ratios of sebacic acid/L-glutamic acid were synthesized. Two kinds of amino-protected glutamic acids, Boc-L-glutamic acid and Z-L-glutamic acid were used to prepare controls that consist of no peptide bonds, denoted as PGSE-B and PGSE-Z, respectively. The prepolymers were characterized using 1H-NMR spectroscopy. Cured elastomers were characterized using FT-IR, DSC, TGA, mechanical testing, and contact angle measurement. In vitro enzymatic degradation of PGSE over a period of 28 days was investigated. FT-IR spectroscopy confirmed the formation of peptide bonds. The glass transition temperature for the elastomer was found to increase as the ratio of sebacic acid/glutamic acid was increased to four. The decomposition temperature of the elastomer decreased as the amount of glutamic acid was increased. PGSE exhibited less stiffness and larger elongation at break as the ratio of sebacic acid/glutamic acid was decreased. Notably, PGSE-Z was stiffer and had smaller elongation at break than PGSE and PGSE-B at the same molar ratio of monomers. The results of in vitro enzymatic degradation demonstrated that PGSE has a lower degradation rate than does PGS, whereas PGSE-B and PGSE-Z degrade at a greater rate than does PGS. SEM images suggest that the degradation of these crosslinked elastomers is due to surface erosion. The cytocompatibility of PGSE was considered acceptable although slightly lower than that of PGS. The altered mechanical properties and retarded degradation kinetics for PGSE reflect the influence of peptide bonds formed by the introduction of L-glutamic acid. PGSE displaying a lower degradation rate compared to that for PGS can be used as a scaffold material for the repair or regeneration of tissues that are featured by a low healing rate.
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