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  • 45233-75-8 Structure
  • Basic information

    1. Product Name: BOC-VAL-GLY-OH
    2. Synonyms: BOC-VAL-GLY-OH;Butoxycarbonyl L-valinyl-glycine;Boc-L-Val-Gly-OH;Boc-Val-Gly-OH≥ 95% (HPLC);(Tert-Butoxy)Carbonyl Val-Gly-OH
    3. CAS NO:45233-75-8
    4. Molecular Formula: C12H22N2O5
    5. Molecular Weight: 274.31
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 45233-75-8.mol
  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: N/A
    3. Flash Point: N/A
    4. Appearance: /
    5. Density: N/A
    6. Refractive Index: 1.479
    7. Storage Temp.: -15°C
    8. Solubility: N/A
    9. CAS DataBase Reference: BOC-VAL-GLY-OH(CAS DataBase Reference)
    10. NIST Chemistry Reference: BOC-VAL-GLY-OH(45233-75-8)
    11. EPA Substance Registry System: BOC-VAL-GLY-OH(45233-75-8)
  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany: 3
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 45233-75-8(Hazardous Substances Data)

45233-75-8 Usage

Chemical Properties

White powder

Check Digit Verification of cas no

The CAS Registry Mumber 45233-75-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 4,5,2,3 and 3 respectively; the second part has 2 digits, 7 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 45233-75:
(7*4)+(6*5)+(5*2)+(4*3)+(3*3)+(2*7)+(1*5)=108
108 % 10 = 8
So 45233-75-8 is a valid CAS Registry Number.
InChI:InChI=1/C12H22N2O5/c1-7(2)9(10(17)13-6-8(15)16)14-11(18)19-12(3,4)5/h7,9H,6H2,1-5H3,(H,13,17)(H,14,18)(H,15,16)

45233-75-8 Well-known Company Product Price

  • Brand
  • (Code)Product description
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  • Detail
  • Aldrich

  • (776564)  Boc-Val-Gly-OH  

  • 45233-75-8

  • 776564-1G

  • 2,432.43CNY

  • Detail
  • Aldrich

  • (776564)  Boc-Val-Gly-OH  

  • 45233-75-8

  • 776564-5G

  • 6,505.20CNY

  • Detail

45233-75-8SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 19, 2017

Revision Date: Aug 19, 2017

1.Identification

1.1 GHS Product identifier

Product name BOC-VAL-GLY-OH

1.2 Other means of identification

Product number -
Other names BOC-Val-Gly

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:45233-75-8 SDS

45233-75-8Relevant articles and documents

Synthesis of tight binding inhibitors and their action on the proprotein- processing enzyme furin

Angliker

, p. 4014 - 4018 (1995)

Furin is a subtilisin-like eukaryotic serine endoprotease which processes proproteins to biologically active proteins and peptides. Also, the envelope proteins of viruses, such as influenza and HIV viruses, need to be processed by furin for infectivity. T

Design, synthesis and preliminary evaluation of α-sulfonyl γ-(glycinyl-amino)proline peptidomimetics as matrix metalloproteinase inhibitors

Zhang, Jian,Li, Xiaoyang,Jiang, Yuqi,Feng, Jinhong,Li, Xiaoguang,Zhang, Yingjie,Xu, Wenfang

, p. 3055 - 3064 (2014/05/20)

A series of novel α-sulfonyl γ-(glycinyl-amino)proline peptidomimetic derivatives were designed, synthesized and assayed for their activities against matrix metalloproteinase-2 (MMP-2), aminopeptidase N (APN)/CD13 and HDACs. The results indicated that all the compounds exhibited highly selective inhibition against MMP-2 as compared with APN and HDACs. The antiproliferative activities of some compounds against SKOV3, HL60 and A549 cells were also investigated. Comparing with the control LY52, compound 12u, with excellent activity both in the enzymatic inhibition assay and cell-based assay, could be used as lead compound for the further development of MMP inhibitors.

Bioinspired modular synthesis of elastin-mimic polymers to probe the mechanism of elastin elasticity

Chen, Yulin,Guan, Zhibin

supporting information; experimental part, p. 4577 - 4579 (2010/06/17)

Bioinspired modular synthesis of elastin-mimic polymers (EMPs) is achieved via Cu-catalyzed alkyne-azide cyclization (CuAAC). By changing the module, EMPs with different secondary structures determined by circular dichroism (CD) spectra in trifluoroethanol (TFE) solution are obtained. The EMPs are characterized by measuring the lower critical solution temperatures (LSCTs) and the bulk mechanic properties under the conditions of both dry and hydrated forms. The unique molecular design enables us to probe mechanistic questions and assess the structure-property relationship of the EMPs. Our results indicate that, instead of a highly organized secondary structure, hydrophobic hydration is critical for the elasticity of EMPs.

N-bromosuccinimide oxidation of dipeptides and their amino acids: Synthesis, kinetics and mechanistic studies

Linge Gowda,Kumara,Channe Gowda,Rangappa

, p. 376 - 385 (2008/02/08)

Dipeptides (DP), namely valyl-glycine (Val-Gly), alanyl-proline (Ala-Pro), and valyl-proline (Val-Pro) were synthesized by classical solution phase methods and characterized. The kinetics of oxidation of amino acids (AA) and DP by N-bromosuccinimide (NBS) was studied in the presence of perchlorate ions in acidic medium at 28°C. The reaction was followed spectrophotometrically at λmax = 240 nm. The reactions follow identical kinetics, being first order each in [NBS], [AA], and [DP]. No effect on [H+], reduction product [succinimide], and ionic strength was observed. Effects of varying dielectric constant of the medium and addition of anions such as chloride and perchlorate were studied. Activation parameters have been computed. The oxidation products of the reaction were isolated and characterized. The proposed mechanism is consistent with the experimental results. An apparent correlation was noted between the rate of oxidation of AA and DP.

Peptide Enolates. C-Alkylation of Glycine Residues in Linear Tri-, Tetra-, and Pentapeptides via Dilithium Azadienediolates

Bossler, Hans G.,Seebach, Dieter

, p. 1124 - 1165 (2007/10/02)

The Boc-protected tripeptides Boc-Val-Gly-Leu-OH (1), Boc-Leu-Sar-Leu-OH (2), Boc-Leu-Gly-MeLeu-OH (3), and Boc-Val-BzlGly-Leu-OMe (64), tetrapeptide Boc-Leu-Gly-Pro-Leu-OH (9), and pentapeptides Boc-Val-Leu-Gly-Abu-Ile-OH (4), Boc-Val-Leu-Sar-MeAbu-Ile-O

Inhibition of human leukocyte elastase (HLE) by N-substituted peptidyl trifluoromethyl ketones

Skiles,Fuchs,Miao,Sorcek,Grozinger,Mauldin,Vitous,Mui,Jacober,Chow,Matteo,Skoog,Weldon,Possanza,Keirns,Letts,Rosenthal

, p. 641 - 662 (2007/10/02)

A series of tripeptides possessing trifluoromethyl or aryl ketone residues at P1 were prepared and evaluated both in vitro and in vivo as potential inhibitors of human leukocyte elastase (HLE). Tripeptides containing non naturally occurring N-substituted glycine residues at the P2-position have been demonstrated to be potent in vitro inhibitors of HLE, with IC50 values in the submicromolar range. Sterically demanding substituents on the P2- nitrogen have no detrimental effect on in vitro potency. The inhibition process presumably acts via hemiketal formation with the active site Ser195 of HLE, and is facilitated by the strongly electron withdrawing trifluoromethyl functionality. Deletion of the amino acid at the P3-subsite region affords inactive compounds. Valine is the preferred residue at the P1-position, whereas the corresponding glycine, alanine, α,α- dimethylglycine, or phenylalanine analogues are all inactive. The compounds described herein all confer a high degree of in vitro specificity when tested against representative cysteine, aspartyl, metallo, and other serine proteases. One of the most potent in vitro inhibitors is (3RS)-N-[4[[[(4- chlorophenyl)sulfonyl]amino]carbonyl]phenyl]oxomethyl]-L-valyl-N-(2,3- dihydro-1H-inden-2-yl)glycine N-[3-(1,1,1-trifluoro-4-methyl-2- oxopentyl)amide (20i; BI-RA-260) (IC50 = 0.084 μM). Compound 20i was also tested in hamsters in an elastase-induced pulmonary hemorrhage (EPH) model. In this model, intratracheal (it.) administration of 20i, 5 min prior to HLE challenge, effectively inhibited hemorrhage in a dose-dependent manner with an ED50 of 4.8 μg. The inhibitor 20i, 20 μg administered it. 24, 48, and 72 h prior to HLE challenge, exhibits significant inhibition against hemorrhage at all time points (97%, 64% and 49%, respectively). In a 21-day chronic model of emphysema in hamsters, 200 μg of HLE administered it. caused an elastase-induced emphysema in the lungs which can be quantitated histologically utilizing image analysis. In this assay, 20i significantly inhibited pulmonary lesions associated with septal destruction and increased alveolar spaces, when dosed at 20 μg it. 5 min prior to challenge with HLE.

Changes in Conformation and Antimicrobial Properties Caused by Replacement of D-Amino Acids with α-Aminoisobutyric Acid in the Gramicidin Backbone: Synthesis and Circular Dichroic Studies

Jelokhani-Niaraki, Masood,Yoshioka, Katsumi,Takahashi, Hiroki,Kato, Fumio,Kondo, Michio

, p. 1187 - 1193 (2007/10/02)

In an attempt to mimic the stable helical structures of proteins with possible pore-forming ability in membranes, the linear gramicidin backbone has been changed by inserting achiral α-aminoisobutyric acids (Aib) in place of all of the alternatively seque

Novel polypeptide and process for producing the same

-

, (2008/06/13)

There are disclosed a novel polypeptide represented by the formula shown below or its acid addition salt or complex: STR1 wherein Ala represents alanine, Ser serine, Leu leucine, Thr threonine, Val valine, Gly glycine, Lys lysine, Gln glutamine, Glu glutamic acid, His histidine, Tyr tyrosine, Pro proline, Arg arginine, Asp aspartic acid, and n represents an integer of 3 to 7, and a process for producing the same comprising forming a peptide or polypeptide represented by the above formula and subjecting the structural units containing a peptide residue represented by the formula: STR2 wherein R represents an active ester residue, Ala, Ser, Leu, Thr and n have the same meanings as defined above, formed in any step of the reaction to cyclization reaction.

Inhibitors of Porcine Pancreatic Elastase. Peptides Incorporating &α-Aza-amino Acid Residues in the P1 Position

Dutta, Anand S.,Giles, Michael B.,Williams, Joseph C.

, p. 1655 - 1664 (2007/10/02)

Inhibitors of porcine pancreatic elastase based on one of the repeating peptide sequences (Gly-Val-Gly-Val-Ala) present in elastin have been prepared.Most of these contain an α-aza-amino acid benzyl ester group at the C-terminus and an N-(1-methoxycarbon

Radioimmunoassay method for determining calcitonin and radioactive tracer for use therein

-

, (2008/06/13)

A hentriacontapeptide of the formula (I) STR1 a radioactive labeled hentriacontapeptide of the formula (I), useful in a radioimmunoassay method and a radioimmunoassay method for determining calcitonin.

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