Boc-Ala(2-Pyr-4-Cl)-OH
Need Assistance?
  • US & Canada:
    +
  • UK: +

Boc-Ala(2-Pyr-4-Cl)-OH

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category
BOC-Amino Acids
Catalog number
BAT-008689
CAS number
2349730-17-0
Molecular Formula
C13H17ClN2O4
Molecular Weight
300.74
IUPAC Name
(2S)-3-(4-chloropyridin-2-yl)-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid
Synonyms
(S)-2-((tert-Butoxycarbonyl)amino)-3-(4-chloropyridin-2-yl)propanoic acid; L-Phenylalanine, chloro-N-[(1,1-dimethylethoxy)carbonyl]-
Density
1.286±0.06 g/cm3
Boiling Point
455.3±45.0 °C at 760 mmHg
InChI
InChI=1S/C13H17ClN2O4/c1-13(2,3)20-12(19)16-10(11(17)18)7-9-6-8(14)4-5-15-9/h4-6,10H,7H2,1-3H3,(H,16,19)(H,17,18)/t10-/m0/s1
InChI Key
PRLVSXCLNKYELE-JTQLQIEISA-N
Canonical SMILES
CC(C)(C)OC(=O)NC(CC1=NC=CC(=C1)Cl)C(=O)O
1. [Peptide derivatives of tylosin-related macrolides]
G A Korshunova, N V Sumbatian, N V Fedorova, I V Kuznetsova, A V Shishkina, A A Bogdanov Bioorg Khim. 2007 Mar-Apr;33(2):235-44. doi: 10.1134/s1068162007020033.
Approaches to the synthesis of model compounds based on the tylosin-related macrolides desmycosin and O-mycaminosyltylonolide were developed using specially designed peptide derivatives of macrolide antibiotics to study the conformation and topography of the nascent peptide chain in the ribosome tunnel. A method for selective bromoacetylation of desmycosin at the hydroxyl group of mycinose was developed, which involves preliminary acetylation of mycaminose. The reaction of the 4"-bromoacetyl derivative of the antibiotic with cesium salts of the dipeptide Boc-Ala-Ala-OH and the hexapeptide MeOTr-Gly-Pro-Gly-Pro-Gly-Pro-OH led to the corresponding peptide derivatives of desmycosin. The protected peptides Boc-Ala-Ala-OH, Boc-Ala-Ala-Phe-OH, and Boc-Gly-Pro-Gly-Pro-Gly-Pro-OH were condensed with the C23-hydroxyl group of O-mycaminosyltylonolide.
2. Correlations between steric/thermochemical parameters and O-/N-acylation reactions of cellulose
Kesavan Devarayan, Taketoshi Hayashi, Masakazu Hachisu, Jun Araki, Kousaku Ohkawa Carbohydr Polym. 2013 Apr 15;94(1):468-78. doi: 10.1016/j.carbpol.2012.12.074. Epub 2013 Jan 16.
N(α)-t-Butyloxycarbonyl (Boc)-amino acids (Xaa = Gly, Ala, or β-Ala) were reacted with the cellulose hydroxyl groups (O-acylation) using N,N'-carbonyl diimidazole. The degrees of substitution toward the total hydroxyl groups (DS%(/OH)s) were 38% for O-(Boc-Gly)-Cellulose, 29% for O-(Boc-Ala)-Cellulose and 53% for O-(Boc-β-Ala)-Cellulose. The one-by-one N-acylation between the O-(Xaa)-Celluloses and Boc-Ala-Gly using a water-soluble carbodiimide yielded the conjugates N-(Boc-Ala-Gly)-Xaa-Celluloses with DS%(/NH2) values of 25% (Xaa = Gly), 35% (Ala), and 48% (β-Ala), respectively. The results were well correlated with ΔG and ΔEstrain profiles, which were predicted by semi-empirical thermochemical parameter calculation coupled with conformer search (R(2)>0.90). N-acylation of the O-(β-Ala)-Cellulose using various length of oligo-peptides, Boc-(Ala-Gly)n and Boc-(Gly-Ala)n (where, n = 0.5, 1.0, 1.5, 2.0, 3.0), suggested that the DS%(/NH2) was dependent on the structural features of the symmetric anhydrides as the N-acylating agents, including conformer populations and their transition energy.
3. Hybrid peptide design. Hydrogen bonded conformations in peptides containing the stereochemically constrained gamma-amino acid residue, gabapentin
Prema G Vasudev, Kuppanna Ananda, Sunanda Chatterjee, Subrayashastry Aravinda, Narayanaswamy Shamala, Padmanabhan Balaram J Am Chem Soc. 2007 Apr 4;129(13):4039-48. doi: 10.1021/ja068910p. Epub 2007 Mar 10.
The crystal structure of 12 peptides containing the conformationally constrained 1-(aminomethyl)cyclohexaneacetic acid, gabapentin (Gpn), are reported. In all the 39 Gpn residues conformationally characterized so far, the torsion angles about the Calpha-Cbeta and Cbeta-Cgamma bonds are restricted to the gauche conformation (+/-60 degrees ). The Gpn residue is constrained to adopt folded conformations resulting in the formation of intramolecularly hydrogen-bonded structures even in short peptides. The peptides Boc-Ac6c-Gpn-OMe 1 and Boc-Gpn-Aib-Gpn-Aib-OMe 2 provide examples of C7 conformation; peptides Boc-Gpn-Aib-OH 3, Boc-Ac6c-Gpn-OH 4, Boc-Val-Pro-Gpn-OH 5, Piv-Pro-Gpn-Val-OMe 6, and Boc-Gpn-Gpn-Leu-OMe 7 provide examples of C9 conformation; peptide Boc-Ala-Aib-Gpn-Aib-Ala-OMe 8 provides an example of C12 conformation and peptides Boc-betaLeu-Gpn-Val-OMe 9 and Boc-betaPhe-Gpn-Phe-OMe 10 provide examples of C13 conformation. Gpn peptides provide examples of backbone expanded mimetics for canonical alpha-peptide turns like the gamma (C7) and the beta (C10) turns. The hybrid betagamma sequences provide an example of a mimetic of the C13 alpha-turn formed by three contiguous alpha-amino acid residues. Two examples of folded tripeptide structures, Boc-Gpn-betaPhe-Leu-OMe 11 and Boc-Aib-Gpn-betaPhg-NHMe 12, lacking internal hydrogen bonds are also presented. An analysis of available Gpn residue conformations provides the basis for future design of folded hybrid peptides.
Online Inquiry
Verification code
Inquiry Basket