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78123-60-1

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78123-60-1 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 78123-60-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,8,1,2 and 3 respectively; the second part has 2 digits, 6 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 78123-60:
(7*7)+(6*8)+(5*1)+(4*2)+(3*3)+(2*6)+(1*0)=131
131 % 10 = 1
So 78123-60-1 is a valid CAS Registry Number.

78123-60-1SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 13, 2017

Revision Date: Aug 13, 2017

1.Identification

1.1 GHS Product identifier

Product name Boc-Leu-Val-Phe-OMe

1.2 Other means of identification

Product number -
Other names methyl (S)-2-<<(tert-butoxycarbonyl)-(S)-leucinyl-(S)-valinyl>amino>-3-phenylpropanoate

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:78123-60-1 SDS

78123-60-1Relevant articles and documents

A peptide based two component white light emitting system

Maiti, Dibakar Kumar,Banerjee, Arindam

, p. 6909 - 6911 (2013/07/26)

A peptide based two component white light emitting system has been designed and developed on the basis of a co-assembly of a PDI containing peptide system as an acceptor and a stilbene containing peptide system as a donor in organic solvents.

Regioselective structural and functional mimicry of peptides. Design of hydrolytically-stable cyclic peptidomimetic inhibitors of HIV-1 protease

Abbenante,March,Bergman,Hunt,Garnham,Dancer,Martin,Fairlie

, p. 10220 - 10226 (2007/10/03)

Hydrolytically-stable cyclic mimetics of the tripeptides Leu-Asn-Phe and Phe-Ile-Val were designed and incorporated into peptidic inhibitors, Ac-{Leu-Asn-Phe}-CHOHCH2-Pro-Ile-Val-NH2 and Ac-Leu-Val-Phe-CHOHCH2-{Phe-Ile-Val}-NH2, of HIV-1 protease. Structural mimicry has been established through molecular modeling and X-ray crystallographic studies of inhibitors bound to HIV-1 protease. Cyclic and acyclic inhibitors had similar conformations that were superimposable and formed similar interactions with the enzyme. Functional mimicry was demonstrated by comparable inhibition of the protease by acyclic and cyclic molecules. Further substitution of the residual acyclic Pro-Ile-Val or Leu-Val-Phe inhibitor components, with Pip-NHtBu or Boc-Phe, respectively, gave hydrolytically stable, water-soluble, lipophilic inhibitors of similar potency. The use of cycles to fix the conformations of amino acid sequences in peptides allows regioselective structural mimicry leading to functional mimicry and also permits localized structure-activity optimization in inhibitors of HIV-1 protease. This approach might be usefully applied to inhibitors of other proteins.

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