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19542-51-9

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19542-51-9 Usage

Chemical Properties

White powder

Check Digit Verification of cas no

The CAS Registry Mumber 19542-51-9 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,9,5,4 and 2 respectively; the second part has 2 digits, 5 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 19542-51:
(7*1)+(6*9)+(5*5)+(4*4)+(3*2)+(2*5)+(1*1)=119
119 % 10 = 9
So 19542-51-9 is a valid CAS Registry Number.
InChI:InChI=1/C22H26N2O5/c1-15(2)19(24-22(28)29-14-17-11-7-4-8-12-17)20(25)23-18(21(26)27)13-16-9-5-3-6-10-16/h3-12,15,18-19H,13-14H2,1-2H3,(H,23,25)(H,24,28)(H,26,27)/t18-,19-/m0/s1

19542-51-9SDS

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 Z-VAL-PHE-OH

1.2 Other means of identification

Product number -
Other names N-Cbz-L-Val-L-Phe

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:19542-51-9 SDS

19542-51-9Relevant articles and documents

A Quick Route to Multiple Highly Potent SARS-CoV-2 Main Protease Inhibitors**

Yang, Kai S.,Ma, Xinyu R.,Ma, Yuying,Alugubelli, Yugendar R.,Scott, Danielle A.,Vatansever, Erol C.,Drelich, Aleksandra K.,Sankaran, Banumathi,Geng, Zhi Z.,Blankenship, Lauren R.,Ward, Hannah E.,Sheng, Yan J.,Hsu, Jason C.,Kratch, Kaci C.,Zhao, Baoyu,Hayatshahi, Hamed S.,Liu, Jin,Li, Pingwei,Fierke, Carol A.,Tseng, Chien-Te K.,Xu, Shiqing,Liu, Wenshe Ray

supporting information, p. 942 - 948 (2020/12/15)

The COVID-19 pathogen, SARS-CoV-2, requires its main protease (SC2MPro) to digest two of its translated long polypeptides to form a number of mature proteins that are essential for viral replication and pathogenesis. Inhibition of this vital pr

Optimization and anti-cancer properties of fluoromethylketones as covalent inhibitors for ubiquitin C-terminal hydrolase L1

Chen, Hao,Das, Chittaranjan,Flaherty, Daniel P.,Galardy, Paul J.,Hewitt, Chad S.,Hussain, Sajjad,Imhoff, Ryan D.,Krabill, Aaron D.,Muli, Christine S.,Wendt, Michael K.

supporting information, (2021/05/31)

The deubiquitinating enzyme (DUB) UCHL1 is implicated in various disease states including neurodegenerative disease and cancer. However, there is a lack of quality probe molecules to gain a better understanding on UCHL1 biology. To this end a study was carried out to fully characterize and optimize the irreversible covalent UCHL1 inhibitor VAEFMK. Structure-activity relationship studies identified modifications to improve activity versus the target and a full cellular characterization was carried out for the first time with this scaffold. The studies produced a new inhibitor, 34, with an IC50 value of 7.7 μM against UCHL1 and no observable activity versus the closest related DUB UCHL3. The molecule was also capable of selectively inhibiting UCHL1 in cells and did not demonstrate any discernible off-target toxicity. Finally, the molecule was used for initial probe studies to assess the role of UCHL1 role in proliferation of myeloma cells and migration behavior in small cell lung cancer cells making 34 a new tool to be used in the biological evaluation of UCHL1.

Side-chain protected oligopeptide fragment condensation using subtilisins in organic solvents

-

Page/Page column 37; 38, (2017/04/11)

Method for enzymatically synthesizing an oligopeptide, comprising the coupling of an (optionally N-protected) protected oligopeptide ester with an (optionally C-protected) protected oligopeptide nucleophile in an organic solvent or an organic solvent mixture having a water content of 0.1 vol % or less, by a subtilisin in any possible form.

Convenient green preparation of dipeptides using unprotected α-amino acids

Ezawa, Tetsuya,Jung, Seunghee,Kawashima, Yuya,Noguchi, Takuya,Imai, Nobuyuki

, p. 75 - 83 (2017/01/10)

Dipeptides and amides were obtained in high yields from N-carbobenzyloxy α-amino acids and 3-phenylpropanoic acid with unprotected α-amino acids via the corresponding mixed carbonic carboxylic anhydrides using ethyl chloroformate and triethylamine by an ecological and convenient method in which the protection of C-terminals is not needed.

Design and synthesis of new tripeptide-type SARS-CoV 3CL protease inhibitors containing an electrophilic arylketone moiety

Konno, Sho,Thanigaimalai, Pillaiyar,Yamamoto, Takehito,Nakada, Kiyohiko,Kakiuchi, Rie,Takayama, Kentaro,Yamazaki, Yuri,Yakushiji, Fumika,Akaji, Kenichi,Kiso, Yoshiaki,Kawasaki, Yuko,Chen, Shen-En,Freire, Ernesto,Hayashi, Yoshio

, p. 412 - 424 (2013/02/25)

We describe here the design, synthesis and biological evaluation of a series of molecules toward the development of novel peptidomimetic inhibitors of SARS-CoV 3CLpro. A docking study involving binding between the initial lead compound 1 and th

Highly diastereoselective peptide chain extensions of unprotected amino acids with N-(Z-α-aminoacyl)benzotriazoles

Katritzky, Alan R.,Suzuki, Kazuyuki,Singh, Sandeep K.

, p. 2645 - 2652 (2007/10/03)

Coupling an unprotected amino acid or dipeptide in partially aqueous solution with a readily available N-(Z-α-amino-acyl)benzotriazole or N-(Z-α-aminopetidoyl)benzotriazole affords N-terminal-protected di-, tri-, and tetrapeptides in yields of 85-98% (average 95% for 2a-i, 93% for 4a-f and 4a′, 86% for 5a-b) with minimal epimerization.

Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: A strategy for the design of peptidase inhibitors

Ganellin, C. Robin,Bishop, Paul B.,Bambal, Ramesh B.,Chan, Suzanne M. T.,Law, James K.,Marabout, Benoit,Luthra, Pratibha Mehta,Moore, Andrew N. J.,Peschard, Olivier,Bourgeat, Pierre,Rose, Christiane,Vargas, Froylan,Schwartz, Jean-Charles

, p. 664 - 674 (2007/10/03)

The cholecystokinin-8 (CCK-8)-inactivating peptidase is a serine peptidase which has been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10). It cleaves the neurotransmitter CCK-8 sulfate at the Met-Gly bond to give Asp-Tyr(SO3H)-Met-OH + Gly-Trp-Met-Asp-Phe-NH2. In seeking a reversible inhibitor of this peptidase, the enzymatic binding subsites were characterized using a fluorimetric assay based on the hydrolysis of the artificial substrate Ala-Ala-Phe-amidomethylcoumarin. A series of di- and tripeptides having various alkyl or aryl side chains was studied to determine the accessible volume for binding and to probe the potential for hydrophobic interactions. From this initial study the tripeptides Ile-Pro-Ile-OH (K(i) = 1 μM) and Ala-Pro-Ala-OH (K(i) = 3 μM) and dipeptide amide Val-Nvl-NHBu (K(i) = 3 μM) emerged as leads. Comparison of these structures led to the synthesis of Val-Pro-NHBu (K(i) = 0.57 μM) which served for later optimization in the design of butabindide, a potent reversible competitive and selective inhibitor of the CCK-8-inactivating peptidase. The strategy for this work is explicitly described since it illustrates a possible general approach for peptidase inhibitor design.

An Effective Water-Free Aprotic System for Dissolving Free Amino Acids

Raydnov, M. G.,Klimenko, L. V.,Mitin, Yu. V.

, p. 283 - 287 (2007/10/03)

An effective water-free system was proposed for dissolution and subsequent use in peptide synthesis of free amino acids and their derivatives. It consists of dimethylformamide, a tertiary base, and inorganic additives. Neutral salts (CF3COONa, Ba(ClO4)2, Ca(ClO4)2, NaClO4, BaI2, or Ca(NO3)2) serve as the inorganic additives that increase the solubility of free amino acids in dimethylformamide and provide true 0.2-3 M amino acid solutions. Triethylamine and N-methylmorpholine are most suitable as the tertiary bases. This system was used in reactions with acylating agents: Boc2O, ZOSu, FmocOSu, and activated derivatives of Nα-protected amino acids or peptides. The corresponding amino acid derivatives or Nα-protected di-, tri-, and tetrapeptides were obtained in yields of 80-99 percent at the reaction times of 30-240 min.

Synthetic Studies on Antifungal Cyclic Peptides, Echinocandins. Stereoselective Total Synthesis of Echinocandin D via a Novel Peptide Coupling

Kurokawa, Natsuko,Ohfune, Yasufumi

, p. 6195 - 6222 (2007/10/02)

Synthetic studies on the novel fungicidal oligopeptides, echinocandins (1b and 1c), are described.The constituent amino acids 5-8 were synthesized in a stereocontrolled manner from the chiral starting materials, 5a, 6a and 7a, respectively.The coupling of these amino acids was characterized by the use of unprotected amino acid as the C-terminal and 2-pyridyl thiol ester as the N-terminal, and the coupling was performed in the presence of 1-(trimethylsilyl)imidazole (TMSIm) or a catalytic amount of tert-amine to give C-terminal free dipeptides, 14 and 16a, respectively, which were converted to the pentapeptide 17a, a common intermediate for the synthesis of 1b and 1c.The synthesis of 1c was achieved by the cyclization of the hexapeptide 24b.

In the search for new anticancer drugs. XXIV: Synthesis and anticancer activity of amino acids and dipeptides containing the 2-chloroethyl- and [N'- (2-chloroethyl)-N'-nitroso]-aminocarbonyl groups

Sosnovsky,Prakash,Rao

, p. 1 - 10 (2007/10/02)

A series of L,L-(42, 44, 46, and 60) and D,D-(43, 45, 47, and 61) dipeptide derivatives composed of phenylglycine, phenylalanine, homophenylalanine, and valine and containing a 2-chloroethylamino group at the C-terminus and an N'-(2-chloroethyl)-N'-nitrosoaminocarbonyl group at the N-terminus of the dipeptides were prepared. The dipeptide derivatives (42- 47, 60, and 61) were first evaluated in vivo for their anticancer activities against the murine lymphocytic leukemia P388. Compounds 42, 44, 46, and 60 possessed activities ranging from 46 to 111 percent increase in life span (%ILS), whereas 43 was marginal (%ILS = 31) and 45, 47, and 61 were inactive. In general, the L,L-series exhibited low to good activity (%ILS = 46-111), whereas the corresponding D,D-series, except for 43 (%ILS = 31), was devoid of activity. The analogously structured monoamino acid derivatives of L- alanine (74), L-phenylalanine (75), and L-aspartic acid (76) exhibited higher activity against P388 than the dipeptide derivatives (i.e., 481, 297, and 481 %ILS, respectively). The more active representatives of dipeptides (i.e., 42, 44, and 60) and the amino acids derivatives 74-76 were then tested in vivo against the murine lymphoid leukemia L1210. Compounds 42, 44, and 60 exhibited either low or marginal activity (i.e., the %ILS values were 46, 31, and 26, respectively). Compounds 74, 75, and 76 possessed low to moderate activity, as evidenced by the %ILS values of 56, 48, and 64, respectively. The %ILS parameters obtained against the P388 and L1210 tumor lines were correlated with the corresponding lipophilicities, and there is a trend towards higher activity with concomitant decrease in hydrophobicity.

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