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Z-(Aib)6-OH, also known as Z-α,α-dimethyl-L-phenylalanyl hexapeptide, is a synthetic peptide composed of six α,α-dimethyl-L-phenylalanine (Aib) residues connected in a linear sequence. The "Z" prefix indicates the presence of a benzyloxycarbonyl (Cbz) protecting group, which is commonly used in peptide synthesis to prevent unwanted side reactions. The hydroxyl group (-OH) at the end of the peptide signifies the presence of a free hydroxyl functional group, which can be used for further chemical modifications or conjugations. This peptide is of interest in the field of chemistry and biochemistry, particularly in the study of peptide conformation, drug design, and the development of novel bioactive compounds.

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  • 4512-44-1 Structure
  • Basic information

    1. Product Name: Z-(Aib)6-OH
    2. Synonyms: Z-(Aib)6-OH
    3. CAS NO:4512-44-1
    4. Molecular Formula:
    5. Molecular Weight: 662.784
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 4512-44-1.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: Z-(Aib)6-OH(CAS DataBase Reference)
    10. NIST Chemistry Reference: Z-(Aib)6-OH(4512-44-1)
    11. EPA Substance Registry System: Z-(Aib)6-OH(4512-44-1)
  • 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: 4512-44-1(Hazardous Substances Data)

4512-44-1 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 4512-44-1 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 4,5,1 and 2 respectively; the second part has 2 digits, 4 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 4512-44:
(6*4)+(5*5)+(4*1)+(3*2)+(2*4)+(1*4)=71
71 % 10 = 1
So 4512-44-1 is a valid CAS Registry Number.

4512-44-1Downstream Products

4512-44-1Relevant 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

, 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

Effect of a strong interfacial electric field on the orientation of the dipole moment of thiolated aib-oligopeptides tethered to mercury on either the N- or C-terminus

Becucci, Lucia,Guryanov, Ivan,Maran, Flavio,Guidelli, Rolando

experimental part, p. 6194 - 6204 (2010/07/04)

Four oligopeptides consisting of a sequence of α-aminoisobutyric acid (Aib) residues, thiolated at either the N- or C-terminus by means of a -(CH2)2-SH anchor, were self-assembled on mercury, which is a substrate known to impart a high fluidity to self-assembled monolayers (SAMs). The surface dipole potential of these peptide SAMs was estimated in 0.1 M KCl aqueous solution at a negatively charged electrode, where the interfacial electric field is directed toward the metal. To the best of our knowledge, this is the first estimate of the surface dipole potential of peptide SAMs in aqueous solution. The procedure adopted consisted in measuring the charge involved in the gradual expansion of a peptide-coated mercury drop and then combining the resulting information with an estimate of the charge density experienced by diffuse layer ions. The dipole moment of the tethered thiolated peptides was found to be directed toward the metal, independent of whether they were thiolated at the C- or N-terminus. This result was confirmed by the effect of these SAMs on the kinetics and thermodynamics of the Eu(III)/Eu(II) redox couple. The combined outcome of these studies indicates that a strong interfacial electric field orients the dipole moment of peptide SAMs tethered to mercury, even against their natural dipole moment.

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