3392-12-9

Basic information

• Product Name: tert-Butoxycarbonyl-L-valine N-hydroxysuccinimide ester
• Synonyms: BOC-L-VALINE HYDROXYSUCCINIMIDE ESTER;BOC-L-VALINE N-HYDROXYSUCCINIMIDE ESTER;BOC-VAL-OSU;BOC-VALINE-OSU;N-ALPHA-T-BOC-L-VALINE N-HYDROXYSUCCINIMIDE ESTER;N-BOC-L-VAL-N-HYDROXYSUCCINIMIDE;N-TERT-BUTOXYCARBONYL-L-VALINE-N-HYDROXYSUCCINIMIDE ESTER;tert-butyl (S)-[1-[[(2,5-dioxopyrrolidin-1-yl)oxy]carbonyl]-2-methylpropyl]carbamate
• CAS NO: 3392-12-9
• Molecular Formula: C₁₄H₂₂N₂O₆
• Molecular Weight: 314.33
• EINECS: 222-236-5
• Product Categories: Amino Acid Derivatives;Amino Acid
• Mol File: 3392-12-9.mol

Chemical Properties

• Melting Point: 126-128 °C
• Appearance: White to off-white/Powder
• Density: 1.223 g/cm³
• Refractive Index: 1.505
• Storage Temp.: −20°C
• PKA: 10.72±0.46(Predicted)
• Sensitive: Moisture Sensitive
• BRN: 1551859
• CAS DataBase Reference: tert-Butoxycarbonyl-L-valine N-hydroxysuccinimide ester(CAS DataBase Reference)
• NIST Chemistry Reference: tert-Butoxycarbonyl-L-valine N-hydroxysuccinimide ester(3392-12-9)
• EPA Substance Registry System: tert-Butoxycarbonyl-L-valine N-hydroxysuccinimide ester(3392-12-9)

Safety Data

• WGK Germany: 3
• F: 3-10-21
• Hazardous Substances Data: 3392-12-9(Hazardous Substances Data)

Usage

Chemical Properties

White powder

InChI:InChI=1/C14H22N2O6/c1-8(2)11(15-13(20)21-14(3,4)5)12(19)22-16-9(17)6-7-10(16)18/h8,11H,6-7H2,1-5H3,(H,15,20)

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 13734-41-3 t-Boc-L-valine 
• 24424-99-5 di-tert-butyl dicarbonate 
• 13734-41-3 (tert-butoxycarbonyl)-L-valine 
• 96935-01-2 Isopropenyl Succinimido Carbonate 
• 72-18-4 L-valine 
• 107960-02-1 1,2,2,2-tetrachloroethyl-(N-succinimidyl)carbonate 

Downstream Products

• 72635-99-5 4-((S)-2-{4-[(S)-2-((S)-2-tert-Butoxycarbonylamino-3-methyl-butyrylamino)-3-methyl-butyrylamino]-3-hydroxy-butyrylamino}-propionylamino)-3-hydroxy-butyric acid 4-nitro-benzyl ester 
• 69209-72-9 (N-tert-butoxycarbonyl-L-valyl)-L-valine 
• 108334-64-1 N-tert-butyloxycarbonyl-L-valyl-L-phenylalanine 
• 86624-62-6 (S)-2-((S)-2-tert-Butoxycarbonylamino-3-methyl-butyrylamino)-5-formylamino-pentanoic acid; compound with dicyclohexyl-amine 
• 33956-18-2 Boc-Val-Lys(Z)-OMe 
• 142811-54-9 ((S)-1-{3,5-Bis-[((S)-2-tert-butoxycarbonylamino-3-methyl-butyrylamino)-methyl]-benzylcarbamoyl}-2-methyl-propyl)-carbamic acid tert-butyl ester 
• 108305-07-3 N^α-t-butyloxycarbonyl-L-valyl-O-acetyl-L-tyrosine 
• 67106-22-3 tert-butyl (S)-1-(benzylamino)-3-methyl-1-oxobutan-2-ylcarbamate 
• 88489-22-9 Boc-L-Val-L-Orn(Z)-L-Leu-OMe 
• 102991-95-7 Boc-Val-Val-Gly-OPac 
• 138850-76-7 Boc-Val-Glu(OBzl)-Glu(OBzl)-Lys(Z)-Ala-Gly-OBzl 
• 111854-54-7 Boc-Val-Gly-Ser(Bzl)-Glu(OBzl)-Ala-Phe-NH₂ 
• 128090-88-0 Boc-Val-Val-Phe-OH 
• 5519-69-7 Boc-Val-Orn(Z)-Leu-D-Phe-Pro-OH 

Relevant articles and documents

2-AMINO-N-(AMINO-OXO-ARYL-LAMBDA6-SULFANYLIDENE)ACETAMIDE COMPOUNDS AND THEIR THERAPEUTIC USE

The present invention pertains generally to the field of therapeutic compounds. More specifically the present invention pertains to certain 2-amino-N-(amino-oxo-aryl-λ6- sulfanylidene)acetamide compounds (referred to herein as ANASIA compounds) that, inter alia, inhibit (e.g., selectively inhibit) bacterial aminoacyl-tRNA synthetase (aaRS) (e.g., bacterial leucyl-tRNA synthetase, LeuRS). The present invention also pertains to pharmaceutical compositions comprising such compounds, and the use of such compounds and compositions, both in vitro and in vivo, to inhibit (e.g., selectively inhibit) bacterial aminoacyl-tRNA synthetase; to treat disorders that are ameliorated by the inhibition (e.g., selective inhibition) of bacterial aminoacyl-tRNA synthetase; to treat bacterial infections; etc.

An optimal “Click” formulation strategy for antibody-drug conjugate synthesis

As a versatile reaction for bioconjugation, Cu(I)-catalyzed alkyne-azide cycloaddition (CuAAC) has enormous potential in the synthesis of antibody-drug conjugates (ADCs). In order to optimize CuAAC-based ADC synthesis, we characterized kinetically different formulation processes by mimicking ADC synthesis using small molecules and subsequently revealed unique kinetic behaviors of different combinations of alkyne and azide conditions. Our results indicate that under ADC synthesis conditions, for an alkyne-containing drug, its concentration has minimal impact on the reaction rate when an antibody has a non-metal-chelating azide but is proportional to concentration when an antibody contains a metal-chelating azide; however, for an alkyne-containing antibody, the ADC synthesis rate is proportional to the concentration of a drug with a non-metal-chelating azide but displays almost no dependence on drug concentration with a metal-chelating azide. Based on our results, we designed and tested an optimal “click” formulation strategy that allowed rapid and cost-effective synthesis of a new ADC.

The antibody-drug conjugate hemiasterlin derivatives and their pharmaceutically (by machine translation)

[Problem] to give one specific target cell cytotoxic, normal cells to the cytotoxic is suppressed, the antibody-drug conjugate medicine hemiasterlin derivatives. (2) Formula [a]:[In the formula, mAb antibody expressed, q is 1 - 8 represents an integer of, h are 1 - 5 represents an integer of, g is an alanine residue (Ala) to represent, g is 1 - 4 represents an integer of, Y is a single bond or a formula (Y-a 1) is represented by the group, Z is formula (Z-a 1), equation (Z-a 2), equation (Z-a 3), formula (Z-a 4), formula (Z-a 5), type (Z-a 6), formula (Za-a 1), equation (Za-in 2), equation (Za-a 3), formula (Za-a 4), formula (Za-a 5), type (Za d 6), formula (Za-a 7), type (Za-in 8), or a group represented by formula (Za-a 10) (Za-a 9) formula a] is expressed by, antibody-drug conjugate or its pharmaceutically acceptable salt containing a drug. [Drawing] no (by machine translation)

Binding and Action of Amino Acid Analogs of Chloramphenicol upon the Bacterial Ribosome

Antibiotic chloramphenicol (CHL) binds with a moderate affinity at the peptidyl transferase center of the bacterial ribosome and inhibits peptide bond formation. As an approach for modifying and potentially improving properties of this inhibitor, we explored ribosome binding and inhibitory activity of a number of amino acid analogs of CHL. The L-histidyl analog binds to the ribosome with the affinity exceeding that of CHL by 10 fold. Several of the newly synthesized analogs were able to inhibit protein synthesis and exhibited the mode of action that was distinct from the action of CHL. However, the inhibitory properties of the semi-synthetic CHL analogs did not correlate with their affinity and in general, the amino acid analogs of CHL were less active inhibitors of translation in comparison with the original antibiotic. The X-ray crystal structures of the Thermus thermophilus 70S ribosome in complex with three semi-synthetic analogs showed that CHL derivatives bind at the peptidyl transferase center, where the aminoacyl moiety of the tested compounds established idiosyncratic interactions with rRNA. Although still fairly inefficient inhibitors of translation, the synthesized compounds represent promising chemical scaffolds that target the peptidyl transferase center of the ribosome and potentially are suitable for further exploration.

MAYTANSINOID DERIVATIVES, CONJUGATES THEREOF, AND METHODS OF USE

Provided herein are maytansinoid derivatives, conjugates thereof, and methods of treating or preventing proliferative diseases with the same.

SITE-SPECIFIC CONJUGATION THROUGH GLYCOPROTEINS LINKAGE AND METHOD THEREOF

A method for specific linkage to a glycoprotein includes obtaining a glycoprotein having a monoglycan or diglycan attached thereto; producing a reactive functional group on a sugar unit on the glycoprotein; and coupling a linker or a payload to the reactive functional group on the glycoprotein.

An efficient and cost-effective approach to kahalalide F N-terminal modifications using a nuisance algal bloom of Bryopsis pennata

Background: Kahalalide F (KF) and its isomer iso-kahalalide F (isoKF), both of which can be isolated from the mollusk Elysia rufescens and its diet alga Bryopsis pennata, are potent cytotoxic agents that have advanced through five clinical trials. Due to a short half-life, narrow spectrum of activity, and a modest response in patients, further efforts to modify the molecule are required to address its limitations. In addition, due to the high cost in producing KF analogues using solid phase peptide synthesis (SPPS), a degradation and reconstruction approach was employed using natural KF from a seasonal algal bloom to generate KF analogues. Methods: N-protected KF was carefully hydrolyzed at the amide linkage between L-Thr12 and D-Val13 using dilute HCl. The synthesis of the C-terminal fragment began with the formation of hexanoic succinimide ester, followed by a reaction with dipeptides. The final coupling reaction was performed between the semisynthesized Fmoc-KF hydrolysis product and the C-terminal fragment, followed by the deprotection of the Fmoc group. Results: Six KF analogues with an addition of an amino acid residue on the N-terminal chain, D-Val14-isoKF (2), Val13-Val14-isoKF (3), D-Leu14-isoKF (4), D-Pro14-isoKF (5), D-Phe14-isoKF (6), and 3,4-2F-D-Phe14-isoKF (7) were prepared using semisynthesis at the exposed N-terminal chain. Conclusions: The overall yield of the medication was 45%. This approach is economical, efficient and amendable to large-scale production while eliminated a nuisance algal bloom. General significance: B. pennata blooms are capable of producing KF in good yields. The semisynthesis from the natural product produced N-terminal modifications for the construction of inexpensive semisynthetic KF libraries.

ANTI-FOLATE RECEPTOR APLHA (FRA) ANTIBODY-DRUG CONJUGATES AND METHODS OF USING THEREOF

The present disclosure provides anti-folate receptor alpha (FRA) antibody-drug conjugates comprising a hydrophilic self-immolative linker. The present disclosures further provide compositions and methods for treating cancers.

HYDROPHILIC SELF-IMMOLATIVE LINKERS AND CONJUGATES THEREOF

The present disclosure provides compounds with a hydrophilic self-immolative linker, which is cleavable under appropriate conditions and incorporates a hydrophilic group to provide better solubility of the compound. The compounds of the present disclosure comprise a drug moiety, a targeting moiety capable of targeting a selected cell population, and a linker which contains an acyl unit, an optional spacer unit for providing distance between the drug moiety and the targeting moiety, a peptide linker which can be cleavable under appropriate conditions, a hydrophilic self-immolative linker, and an optional second self-immolative spacer or cyclization self-elimination linker.

PRODRUGS OF GUANFACINE

Prodrugs of guanfacine with amino acids or short peptides, pharmaceutical compositions containing such prodrugs and a method for providing therapeutic benefit in the treatment of ADHD/ODD (attention deficient hyperactivity disorder and oppositional defiance disorder) with guanfacine prodrugs are provided herein. Additionally, methods for minimizing or avoiding the adverse gastrointestinal side effects associated with guanfacine administration, as well as improving the pharmacokinetics of guanfacine are provided herein.