36360-61-9

Basic information

• Product Name: BOC-NLE-OSU
• Synonyms: BOC-NLE-OSU;BOC-NORLEUCINE-OSU;BOC-L-NORLEUCINE HYDROXYSUCCINIMIDE ESTER;BOC-L-NORLEUCINE N-HYDROXYSUCCINIMIDE ESTER;BOC-L-2-AMINOHEXANOIC ACID-N-HYDROXYSUCCINIMIDE ESTER;BOC-L-2-AMINOHEXANOIC ACID-OSU;BOC-L-NORLEUCINE HYDROXYSUCCINIMIDESTER
• CAS NO: 36360-61-9
• Molecular Formula: C₁₅H₂₄N₂O₆
• Molecular Weight: 328.36
• Mol File: 36360-61-9.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: BOC-NLE-OSU(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-NLE-OSU(36360-61-9)
• EPA Substance Registry System: BOC-NLE-OSU(36360-61-9)

Safety Data

• Hazardous Substances Data: 36360-61-9(Hazardous Substances Data)

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 6404-28-0 Boc-Nle-OH 

Downstream Products

• 25691-61-6 Boc-Nle-Gly-Trp-Met-Asp-Phe-NH₂ 
• 115044-09-2 Boc-Nle-Gly-OCp 
• 121888-49-1 Boc-Tyr-Nle-Gly-Trp-Nle-Asp-gPhe-For 
• 121959-93-1 Boc-Tyr-Nle-Gly-D-Trp-Nle-Asp-gPhe-For 
• 121959-92-0 Z-D-Trp-Nle-Asp(OBzl)-gPhe-For 
• 121888-48-0 Z-Trp-Nle-Asp(OBzl)-gPhe-For 
• 121888-43-5 Boc-Tyr-Nle-gGly-D-Trp-D-Nle-D-Asp(OBzl)-Z 
• 121888-45-7 Boc-Tyr-Nle-gGly-D-Trp-D-Nle-D-Asp-COCH₂CH₂C₆H₅ 
• 121888-42-4 Boc-Nle-gGly-D-Trp-D-Nle-D-Asp(OBzl)-Z 
• 121888-41-3 Boc-Nle-gGly-D-Trp-D-Nle-Z 
• 121888-40-2 Boc-Nle-gGly-D-Trp-Z 
• 121888-30-0 Boc-Tyr(SO₃K)-Nle-Gly-Trp-Nle-Asp-gPhe-For 
• 121888-29-7 Boc-Tyr(SO₃K)-Nle-gGly-D-Trp-D-Nle-D-Asp-COCH₂CH₂C₆H₅ 
• 151036-40-7 N^α-(tert-butyloxycarbonyl)-L-norleucyl-L-aspartic acid β-benzyl ester 

Relevant articles and documents

Transformation of gold(I)-cyclo[-Met-Met-] complex supramolecular fibers into aligned gold nanoparticles

A cyclic dipeptide cyclo[L-methionylL- methionyl] and gold(I) cation were found to form a complex in a 1:2 ratio. Pouring a DMF solution of the complex into ethyl acetate afforded fibers with lengths of more than 20 μm and 100400nm in width, which consisted of fibrous nanostructures 50100nm in diameter. Treatment of this supramolecular fiber with catechol gave linearly aligned Au nanoparticles on the original fibers.

Specificity of lysine: N6-hydroxylase: A hypothesis for a reactive substrate intermediate in the catalytic mechanism

The recombinant cytoplasmic preparation of lysine: N6-hydroxylase catalyzes the conversion of L-lysine to its N6-hydroxy derivative when supplemented with the cofactors NADPH and FAD. A number of lysine analogs reflecting minor alterations in the inherent structural features of the amino acid as well compounds with relatively high affinity for lysine binding domains in other proteins were examined for their ability to serve as substrates of lysine: N6-hydroxylase. These studies have revealed that the enzyme does not tolerate any change in the structural features of L-lysine, its preferred substrate, with the exception of the replacement of the C(γ)H2-methylene group by sulfur, as in (S)-2-aminoethyl-L-cysteine. L-Norleucine is a potent inhibitor of the enzyme while L-norvaline and L-α-aminobutyric acid do not exhibit such effect, indicating the importance of a C4 hydrophobic side chain for effective interaction with the enzyme. Among the N-alkyl amides of hydrophobic amino acids, only L-norleucine methylamide and L-α-aminobutyric acid ethylamide serve as moderate inhibitors of lysine: N6-hydroxylase. Based on the enzyme's stringent substrate specificity, a mechanism involving the conversion of L-lysine to 2-aminocaprolactam prior to its oxygenation by the 4α-peroxyflavin intermediate in the catalytic cycle is proposed.