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Alanine, 2-methyl-N-[(phenylmethoxy)carbonyl]alanyl-2-methyl-, 1,1-dimethylethyl ester is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

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  • Alanine, 2-methyl-N-[(phenylmethoxy)carbonyl]alanyl-2-methyl-, 1,1-dimethylethyl ester

    Cas No: 83537-94-4

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  • 83537-94-4 Structure
  • Basic information

    1. Product Name: Alanine, 2-methyl-N-[(phenylmethoxy)carbonyl]alanyl-2-methyl-, 1,1-dimethylethyl ester
    2. Synonyms:
    3. CAS NO:83537-94-4
    4. Molecular Formula: C20H30N2O5
    5. Molecular Weight: 378.469
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 83537-94-4.mol
  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: N/A
    3. Flash Point: N/A
    4. Appearance: N/A
    5. Density: N/A
    6. Refractive Index: N/A
    7. Storage Temp.: N/A
    8. Solubility: N/A
    9. CAS DataBase Reference: Alanine, 2-methyl-N-[(phenylmethoxy)carbonyl]alanyl-2-methyl-, 1,1-dimethylethyl ester(CAS DataBase Reference)
    10. NIST Chemistry Reference: Alanine, 2-methyl-N-[(phenylmethoxy)carbonyl]alanyl-2-methyl-, 1,1-dimethylethyl ester(83537-94-4)
    11. EPA Substance Registry System: Alanine, 2-methyl-N-[(phenylmethoxy)carbonyl]alanyl-2-methyl-, 1,1-dimethylethyl ester(83537-94-4)
  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 83537-94-4(Hazardous Substances Data)

83537-94-4 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 83537-94-4 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,3,5,3 and 7 respectively; the second part has 2 digits, 9 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 83537-94:
(7*8)+(6*3)+(5*5)+(4*3)+(3*7)+(2*9)+(1*4)=154
154 % 10 = 4
So 83537-94-4 is a valid CAS Registry Number.

83537-94-4SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 16, 2017

Revision Date: Aug 16, 2017

1.Identification

1.1 GHS Product identifier

Product name Z-Aib-Aib-O(t-Bu)

1.2 Other means of identification

Product number -
Other names Z-Aib-Aib-OtBu

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:83537-94-4 SDS

83537-94-4Relevant articles and documents

Helical Peptides Design for Molecular Dipoles Functionalization of Wide Band Gap Oxides

Bartynski, Robert A.,Chen, Yuan,Galoppini, Elena,Harmer, Ryan,Rangan, Sylvie,Viereck, Jonathan

supporting information, p. 3489 - 3498 (2020/03/06)

The use of helical hexapeptides to establish a surface dipole layer on a TiO2 substrate, with the goal of influencing the energy levels of a coadsorbed chromophore, is explored. Two helical hexapeptides, synthesized from 2-amino isobutyric acid

Conformation-specific spectroscopy of capped, gas-phase Aib oligomers: Tests of the Aib residue as a 310-helix former

Gord, Joseph R.,Hewett, Daniel M.,Hernandez-Castillo, Alicia O.,Blodgett, Karl N.,Rotondaro, Matthew C.,Varuolo, Adalgisa,Kubasik, Matthew A.,Zwier, Timothy S.

, p. 25512 - 25527 (2016/09/23)

The conformational preferences of a series of capped peptides containing the helicogenic amino acid aminoisobutyric acid (Aib) (Z-Aib-OH, Z-(Aib)2-OMe, and Z-(Aib)4-OMe) are studied in the gas phase under expansion-cooled conditions. Aib oligomers are known to form 310-helical secondary structures in solution and in the solid phase. However, in the gas phase, accumulation of a macrodipole as the helix grows could inhibit helix stabilization. Implementing single-conformation IR spectroscopy in the NH stretch region, Z-Aib-OH and Z-(Aib)2-OMe are both observed to have minor conformations that exhibit dihedral angles consistent with the 310-helical portion of the Ramachandran map (φ, ψ = -57°, -30°), even though they lack sufficient backbone length to form 10-membered rings which are a hallmark of the developed 310-helix. For Z-(Aib)4-OMe three conformers are observed in the gas phase. Single-conformation infrared spectroscopy in both the NH stretch (Amide A) and CO stretch (Amide I) regions identifies the main conformer as an incipient 310-helix, having two free NH groups and two C10 H-bonded NH groups, labeled an F-F-10-10 structure, with a calculated dipole moment of 13.7 D. A second minor conformer has an infrared spectrum characteristic of an F-F-10-7 structure in which the third and fourth Aib residues have φ, ψ = 75°, -74° and -52°, 143°, Ramachandran angles which fall outside of the typical range for 310-helices, and a dipole moment that shrinks to 5.4 D. These results show Aib to be a 310-helix former in the gas phase at the earliest stages of oligomer growth.

Deracemization and the first CD spectrum of a 310-helical peptide made of achiral α-amino-isobutyric acid residues in a chiral membrane mimetic environment

Ceccacci, Francesca,Mancini, Giovanna,Rossi, Paola,Scrimin, Paolo,Sorrenti, Alessandro,Tecilla, Paolo

, p. 10133 - 10135 (2013/10/22)

Interaction of the racemic helical homo-octapeptide made by the achiral Cα-methyl alanine (Aib) amino acid with a chiral enantiopure micellar aggregate made of N-dodecylproline led to the deracemization of the helical Aib sequence thus allowing

Peptide fragment coupling using a continuous-flow photochemical rearrangement of nitrones

Zhang, Yuan,Blackman, Melissa L.,Leduc, Andrew B.,Jamison, Timothy F.

, p. 4251 - 4255 (2013/05/08)

Go with the flow: A general approach for amide bond formation by way of a continuous-flow photochemical rearrangement of nitrones was described (see scheme). Simple aryl-alkyl amide bonds as well as complex peptide bonds were constructed efficiently with a residence time less than 20minutes. A tetrapeptide was synthesized in this way and the method could be applied to peptide fragment coupling. Copyright

Rational design of gold(III)-dithiocarbamato peptidomimetics for the targeted anticancer chemotherapy

Kouodom, Morelle Negom,Boscutti, Giulia,Celegato, Marta,Crisma, Marco,Sitran, Sergio,Aldinucci, Donatella,Formaggio, Fernando,Ronconi, Luca,Fregona, Dolores

, p. 248 - 260 (2013/01/15)

As a further extension of our research work focusing on the development of gold(III)-dithiocarbamato dtc derivatives of oligopeptides as potential anticancer agents, complexes [AuIIIX2(dtc-Sar-l-Ser(t-Bu)- O(t-Bu))] (X = Br (1a)/Cl (

Emerimicins III and IV and their ethylalanine12 epimers. Facilitated chemical-enzymatic synthesis and a qualitative evaluation of their solution structures

Slomczynska, Urszula,Beusen, Denise D.,Zabrocki, Janusz,Kociolek, Karol,Redlinski, Adam,Rensser, Fritz,Hutton, William C.,Leplawy, Miroslaw T.,Marshall, Garland R.

, p. 4095 - 4106 (2007/10/02)

The peptaibol antibiotics, emerimicin III and IV (Ac-Phe1-MeA2-MeA3-MeA4-VaI 5-Gly6-Leu7-MeA8-MeA 9-Hyp10-Gln11-R-EtA12-Hyp

Determination of an 8-? interatomic distance in a helical peptide by solid-state NMR spectroscopy

Holl, Susan M.,Marshall, Garland R.,Beusen, Denise D.,Kociolek, Karol,Redlinski, Adam S.,Leplawy, Miroslaw T.,McKay, Robert A.,Vega, Shimon,Schaefer, Jacob

, p. 4830 - 4833 (2007/10/02)

The combination of transferred-echo double resonance (TEDOR) with rotational-echo double resonance (REDOR) has been used to measure an 8-? fluorine-carbon internuclear distance in a nine-residue fragment of the peptide antibiotic emerimicin. The fragment is 19FCH2CO-Phe-MeA-MeA-[1-13C]MeA-[ 15N]Val-Gly-Leu-MeA-MeA-OBzl (MeA = α-methylalanine or aminoisobutyric acid). The TEDOR part of this magic-angle-spinning, solid-state NMR experiment selects the 13C label by its dipolar coupling to 15N and suppresses the natural-abundance carbon background. The REDOR part of the experiment measures dipolar coupling of the selected carbon to 19F. The TEDOR-REDOR combined experiment works with a variety of spin 1/2 nuclei and can be used to characterize internuclear distances and geometry in macromolecular aggregates that do not crystallize.

SYNTHESE VON 2-METHYLALANIN-PEPTIDEN, DIE pH-ABHAENGIGKEIT IHRER 13C-NMR-SPECTREN UND EINE NEUE METHODE ZUR AUSWERTUNG UEBER CS-DIAGRAMME

Leibfritz, Dieter,Haupt, Erhard,Dubischar, Norbert,Lachmann, Heinrich,Oekonomopulos, Raymond,Jung, Guenther

, p. 2165 - 2182 (2007/10/02)

The uncommon amino-acid 2-methylalanine (α-aminoisobutiryc acid, Aib) was investigated by 13C-NMR.The chemical shifts of amino- or carboxy-protected derivates of Aib and of protected oligopeptides are discussed with respect to neighbouring groups and amino acids.The pH-dependence of the 13C-NMR spectra of Aib, Aib-Ala, Ala-Aib, Aib-Ala-Aib and Aib-Ala-Aib-Ala-Aib was studied.Using these examples, a new and advantageous method is demonstrated for the first time for the evaluation of NMR titration curves, which uses so-called chemical shift diagrams (CS diagrams).

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