32886-55-8

Basic information

• Product Name: BOC-GLU(OTBU)-OSU
• Synonyms: BOC-GLUTAMIC ACID(OTBU)-OSU;BOC-GLU(OTBU)-OSU;BOC-L-GLUTAMIC ACID-GAMMA-T-BUTYL-ALPHA-HYDROXYSUCCINIMIDE DIESTER;BOC-L-GLUTAMIC ACID-GAMMA-T-BUTYL ESTER ALPHA-N-HYDROXYSUCCINIMIDE ESTER;N-ALPHA-T-BOC-L-GLUTAMIC ACID GAMMA-T-BUTYL ESTER N-HYDROXYSUCCINIMIDE ESTER;N-ALPHA-T-BOC-L-GLUTATMIC ACID GAMMA-T-BUTYL ESTER N-HYDROXYSUCCINIMIDE ESTER;BOC-L-GLUTAMIC ACID-Y-T-BUTYL-A-HYDROXYSUCCINIMID-DIESTER;(S)-5-tert-Butyl 1-(2,5-dioxopyrrolidin-1-yl) 2-((tert-butoxycarbonyl)aMino)pentanedioate
• CAS NO: 32886-55-8
• Molecular Formula: C₁₈H₂₈N₂O₈
• Molecular Weight: 400.42
• Mol File: 32886-55-8.mol

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: BOC-GLU(OTBU)-OSU(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-GLU(OTBU)-OSU(32886-55-8)
• EPA Substance Registry System: BOC-GLU(OTBU)-OSU(32886-55-8)

Safety Data

• Hazardous Substances Data: 32886-55-8(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
BOC-GLU(OTBU)-OSU serves as a key component in the synthesis of peptides for drug development, facilitating the creation of new pharmaceuticals with targeted therapeutic effects. Its protective groups ensure the stability and specificity required for complex peptide assembly, enhancing the efficiency and success of peptide-based drug synthesis.
Used in Biochemical Research:
In the realm of biochemical research, BOC-GLU(OTBU)-OSU is employed as a fundamental building block for the construction of complex peptide sequences. Its role in the synthesis process aids scientists in exploring the structure-function relationships of peptides, thereby advancing understanding in areas such as protein function, enzyme activity, and signal transduction pathways.
Used in Peptide Synthesis Education:
BOC-GLU(OTBU)-OSU is also utilized as an educational tool in teaching laboratories, where students learn the principles of peptide synthesis and the importance of protecting groups in organic chemistry. This hands-on experience is crucial for training the next generation of chemists and biochemists in the intricacies of peptide synthesis techniques.

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 13726-84-6 Boc-Glu(OtBu)-OH 

Downstream Products

• 1239116-67-6 (S)-Boc-Glu(Ot-Bu)-NHBn 
• 1260020-43-6 N-Boc-(S)-glutamic acid (tert-butyl ester)-mexiletine 
• 1260020-44-7 mexiletine-(S)-glutamic acid amide hydrochloride 
• 1009103-03-0 C₃₈H₅₀ClN₅O₁₁S 
• 192052-72-5 Boc-Glu(O^tBu)-Tyr[CO(CH₂)4CO-bzoc⁶A(=CMe₂)]-Leu-morpholine 
• 192052-65-6 C₅₆H₇₀N₈O₁₆S 
• 192052-62-3 4-{4-[(S)-2-((S)-1-Benzyloxycarbonyl-3-methyl-butylcarbamoyl)-2-((S)-4-tert-butoxycarbonyl-2-tert-butoxycarbonylamino-butyrylamino)-ethyl]-phenoxysulfonyl}-2-hydroxy-benzoic acid 
• 192052-58-7 4-{4-[(S)-2-((S)-1-Benzyloxycarbonyl-3-methyl-butylcarbamoyl)-2-((S)-4-tert-butoxycarbonyl-2-tert-butoxycarbonylamino-butyrylamino)-ethyl]-phenoxysulfonyl}-benzoic acid 
• 192052-56-5 (S)-4-tert-Butoxycarbonylamino-4-{(S)-2-(4-hydroxy-phenyl)-1-[(S)-3-methyl-1-(morpholine-4-carbonyl)-butylcarbamoyl]-ethylcarbamoyl}-butyric acid tert-butyl ester 
• 192052-55-4 (S)-2-[(S)-2-((S)-4-tert-Butoxycarbonyl-2-tert-butoxycarbonylamino-butyrylamino)-3-(4-hydroxy-phenyl)-propionylamino]-4-methyl-pentanoic acid 
• 192052-54-3 (S)-2-[(S)-2-((S)-4-tert-Butoxycarbonyl-2-tert-butoxycarbonylamino-butyrylamino)-3-(4-hydroxy-phenyl)-propionylamino]-4-methyl-pentanoic acid benzyl ester 

Relevant articles and documents

Ynamide-Mediated Thiopeptide Synthesis

Exploration of the full potential of thioamide substitution as a tool in the chemical biology of peptides and proteins has been hampered by insufficient synthetic strategies for the site-specific introduction of a thioamide bond into a peptide backbone. A novel ynamide-mediated two-step strategy for thiopeptide bond formation with readily available monothiocarboxylic acids as thioacyl donors is described. The α-thioacyloxyenamide intermediates formed from the ynamides and monothiocarboxylic acids can be purified, characterized, and stored. The balance between their activity and stability enables them to act as effective thioacylating reagents to afford thiopeptide bonds under mild reaction conditions. Amino acid functional groups such as OH, CONH2, and indole NH groups need not be protected during thiopeptide synthesis. The modular nature of this strategy enables the site-specific incorporation of a thioamide bond into peptide backbones in both solution and the solid phase.

Functional profiling of adenylation domains in nonribosomal peptide synthetases by competitive activity-based protein profiling

We describe competitive activity-based protein profiling (ABPP) to accelerate the functional prediction and assessment of adenylation (A) domains in nonribosomal peptide synthetases (NRPSs) in proteomic environments. Using a library of sulfamoyloxy-linked aminoacyl-AMP analogs, the competitive ABPP technique offers a simple and rapid assay system for adenylating enzymes and provides insight into enzyme substrate candidates and enzyme active-site architecture.