77302-72-8

Basic information

• Product Name: BOC-L-2-AMINOADIPIC ACID
• Synonyms: BOC-L-ALPHA-AMINOADIPIC ACID;BOC-L-2-AMINOADIPIC ACID;BOC-L-HOMOGLUTAMIC ACID;BOC-AAD-OH;N-BOC-L-2-AMINOADIPIC ACID;N-ALPHA-BUTOXYCARBONYL-L-ALPHA-AMINOADIPIC ACID;NALPHA-tert-Butoxycarbonyl-L-2-aminoadipic acid;Boc-L-homoglutamic acid, N-Boc-L-2-aminoadipic acid
• CAS NO: 77302-72-8
• Molecular Formula: C₁₁H₁₉NO₆
• Molecular Weight: 261.27
• Product Categories: amino acid;amino acids
• Mol File: 77302-72-8.mol

Chemical Properties

• Melting Point: 121-122℃
• Boiling Point: 462.1°C at 760 mmHg
• Flash Point: 233.3°C
• Appearance: /
• Density: 1.231g/cm³
• Vapor Pressure: 8.04E-10mmHg at 25°C
• Refractive Index: 1.491
• Storage Temp.: Store at 0°C
• PKA: 3.93±0.21(Predicted)
• CAS DataBase Reference: BOC-L-2-AMINOADIPIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-L-2-AMINOADIPIC ACID(77302-72-8)
• EPA Substance Registry System: BOC-L-2-AMINOADIPIC ACID(77302-72-8)

Safety Data

• WGK Germany: 3
• HazardClass: IRRITANT
• Hazardous Substances Data: 77302-72-8(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
BOC-L-2-AMINOADIPIC ACID is used as a key building block for the synthesis of complex molecules, contributing to the development of new drugs and therapeutic agents. Its enhanced stability and solubility, due to the BOC protecting group, make it an advantageous component in drug formulation and production processes.
Used in Biotechnology Industry:
In the biotechnology field, BOC-L-2-AMINOADIPIC ACID serves as an essential component in the creation of peptides and proteins with specific functions. Its role in the synthesis of these biologically active molecules supports research and development in areas such as protein engineering, enzyme production, and the design of novel biotherapeutics.
Used in Peptide and Protein Synthesis:
BOC-L-2-AMINOADIPIC ACID is utilized as a starting material in the synthesis of peptides and proteins. The BOC protecting group ensures that the compound remains stable during the synthesis process, allowing for the creation of well-defined and functional peptide and protein structures.
Used in Research and Development:
BOC-L-2-AMINOADIPIC ACID is employed as a research tool in academic and industrial laboratories. Its unique properties and reactivity make it suitable for investigating various biological processes, testing new synthetic methods, and exploring potential applications in drug discovery and development.

InChI:InChI=1/C11H19NO6/c1-11(2,3)18-10(17)12-7(9(15)16)5-4-6-8(13)14/h7H,4-6H2,1-3H3,(H,12,17)(H,13,14)(H,15,16)/t7-/m0/s1

Upstream product

• 124747-27-9 (S)-2-tert-Butoxycarbonylamino-succinic acid 1-benzyl ester 4-(2-thioxo-2H-pyridin-1-yl) ester 
• 30925-18-9 2-tert-butoxycarbonylamino-succinic acid 1-benzyl ester 
• 108312-38-5 N^α,N^ε-di-tert-butyloxycarbonyl-L-lysine 2,2,2-trichloroethyl ester 
• 108312-35-2 N^α,N^ca-di-tert-butyloxycarbonyl-L-homoglutamine 
• 110545-04-5 (S)-2,6-Bis-tert-butoxycarbonylamino-6-oxo-hexanoic acid 2,2,2-trichloro-ethyl ester 
• 97347-42-7 (+)-(S)-N₂,N₆-bis[(1,1-dimethylethoxy)carbonyl]-6-oxo-lysine methyl ester 
• 115572-96-8 (S)-2-tert-Butoxycarbonylamino-5-(pyridin-2-ylsulfanyl)-hexanedioic acid 1-benzyl ester 6-methyl ester 
• 1118-90-7 L-homoglutamic acid 
• 24424-99-5 di-tert-butyl dicarbonate 

Downstream Products

• 77611-37-1 (S)-2-((tert-butoxycarbonyl)amino)-6-hydroxyhexanoic acid 
• 790244-48-3 (S)-5-((R)-2-Benzhydrylsulfanyl-1-carboxy-ethylcarbamoyl)-2-tert-butoxycarbonylamino-pentanoic acid 4-methoxy-benzyl ester 
• 790244-47-2 N-tert-butyloxycarbonyl-L-α-aminoadipic acid α-p-methoxybenzyl ester 
• 1118-90-7 L-homoglutamic acid 
• 110544-98-4 (2S)-5-benzyloxycarbonyl-2-(tert-butoxycarbonyl)aminopentanoic acid dicyclohexylammonium salt 

Relevant articles and documents

The Interaction of Isopenicillin N Synthase with Homologated Substrate Analogues δ-(L-α-Aminoadipoyl)-L-homocysteinyl-D-Xaa Characterised by Protein Crystallography

Isopenicillin N synthase (IPNS) converts the linear tripeptide δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (ACV) into bicyclic isopenicillin N (IPN) in the central step in the biosynthesis of penicillin and cephalosporin antibiotics. Solution-phase incubation experiments have shown that IPNS turns over analogues with a diverse range of side chains in the third (valinyl) position of the substrate, but copes less well with changes in the second (cysteinyl) residue. IPNS thus converts the homologated tripeptides δ-(L-α-aminoadipoyl)-L-homocysteinyl-D-valine (AhCV) and δ-(L-α-aminoadipoyl)-L-homocysteinyl-D-allylglycine (AhCaG) into monocyclic hydroxy-lactam products; this suggests that the additional methylene unit in these substrates induces conformational changes that preclude second ring closure after initial lactam formation. To investigate this and solution-phase results with other tripeptides δ-(L-α-aminoadipoyl)-L-homocysteinyl-D-Xaa, we have crystallised AhCV and δ-(L-α-aminoadipoyl)-L-homocysteinyl-D-S-methylcysteine (AhCmC) with IPNS and solved crystal structures for the resulting complexes. The IPNS:FeII:AhCV complex shows diffuse electron density for several regions of the substrate, revealing considerable conformational freedom within the active site. The substrate is more clearly resolved in the IPNS:FeII:AhCmC complex, by virtue of thioether coordination to iron. AhCmC occupies two distinct conformations, both distorted relative to the natural substrate ACV, in order to accommodate the extra methylene group in the second residue. Attempts to turn these substrates over within crystalline IPNS using hyperbaric oxygenation give rise to product mixtures. Loose fit: IPNS catalyses the central step in penicillin biosynthesis. Substrate analogues containing L-homocysteine in place of the natural substrate's L-cysteine residue are not converted into bicyclic products. Crystal structures for IPNS complexes with two such analogues reveal that the additional CH2 unit affords considerable conformational freedom when these analogues bind to IPNS. Copyright

Controlling the position of functional groups at the liquid/solid interface: Impact of molecular symmetry and chirality

With the aim of controlling the position of functional groups in a substrate-supported monolayer, a new family of functionalized linear alkyl chains was designed and synthesized, aided by molecular mechanics and dynamics simulations of its two-dimensional self-assembly on graphite. The self-assembly of these amino functionalized diamides at the liquid/solid interface was investigated with scanning tunneling microscopy. Intermolecular hydrogen-bonding interactions involving amides, combined with the effect of molecular symmetry and chirality, were found to guide the self-assembly. Control of the relative position and orientation of the amine groups was achieved, in the case of enantiopure compounds. Interestingly, racemates led to both racemic conglomerate and solid solution formation, with a concomitant loss of positional and orientational control of the amino groups as a result.

ALBUMIN-BINDING COMPOUNDS

The present invention provides an albumin-binding compound essentially of the following elements: a spacer group, a water-soluble bridging group, a fatty acid chain and an acidic group characterised in that the acidic group is attached to the distal end of the fatty acid chain. The invention also provides an albumin-binding compound to which one or more biologically active moieties are attached.

Crystallographic studies on the reaction of isopenicillin N synthase with an unsaturated substrate analogue

Isopenicillin N synthase (IPNS) catalyses conversion of the linear tripeptie δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (ACV) to isopenicillin N (IPN), the central step in biosynthesis of the β-lactam antibiotics. The unsaturated substrate analogue δ-(L-α-aminoadipoyl)-L-cysteinyl-D-vinylglycine (ACvG) has previously been incubated with IPNS and a single product was isolated, a 2-α-hydroxymethyl isopenicillin N (HMPen), formed via a monooxygenase mode of reactivity. ACvG has now been crystallised with IPNS and the structure of the anaerobic IPNS:Fe(II):ACvG complex determined to 1.15 A resolution. Furthermore, by exposing the anaerobically grown crystals to high-pressure oxygen gas, a structure corresponding to the bicyclic product HMPen has been obtained at 1.60 A resolution. In light of these and other IPNS structures, and recent developments with related dioxygenases, the [2 + 2] cycloaddition mechanism for HMPen formation from ACvG has been revised, and a stepwise radical mechanism is proposed. This revised mechanism remains consistent with the observed stereospecificity of the transformation, but fits better with apparent constraints on the coordination geometry around the active site iron atom.

PROPERTIES OF Nα,Nca-DI-TERT-BUTYLOXYCARBONYL-ω-CARBAMOYL-α-AMINO ACIDS AND DIRECT SYNTHESIS OF PROTECTED HOMOGLUTAMIC ACID DERIVATIVES

The protected carboxamide function of Nα,Nca-di-tert-butyloxy-carbonyl-ω-carbamoyl-α-amino acids worked well with nucleophilic reagents.Applying this novel reactivity, we developed an efficient synthetic route to Nα-tert-butyloxycarbonylhomoglutamic acid and its derivatives, including Nα-tert-butyloxycarbonylhomoglutamic acid δ-benzyl ester, from Nα,Nca-di-tert-butyloxycarbonylhomoglutamine.KEYWORDS - protected homoglutamic acid synthesis; Nca-tert-butyloxycarbonylated carboxamide; hydrolysis; selective deprotection; Nα-tert-butyloxycarbonylhomoglutamic acid δ-benzyl ester; Nα-tert-butyloxycarbonylhomoglutamic acid α-tert-butyl ester; Nα-tert-butyloxycarbonylhomoglutamine; optical purity

Synthesis of Retrohydroxamate Analogues of the Microbial Iron-Transport Agent Ferrichrome

A retrohydroxamate analogue (2) of the peptidyl iron transport agent ferrichrome 1 has been prepared in which transposition of the hydroxamate functionalities in the respective amino acid side chains, as compared to ferrichrome, has been effected.The requ