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Enantiomeric resolution and modeling of DL ‐alanine‐ DL ‐tryptophan dipeptide on amylose stationary phase
Author(s) -
Ali Imran,
Khattab Raffat A.,
Alothman Zeid A.,
Badjah Ahmad Yacine,
Alwarthan Abdulrahman
Publication year - 2018
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.22813
Subject(s) - chemistry , enantiomer , dipeptide , amylose , resolution (logic) , chromatography , elution , tryptophan , alanine , stereochemistry , peptide , organic chemistry , amino acid , biochemistry , artificial intelligence , starch , computer science
The enantiomeric resolution of DL‐alanine‐DL‐tryptophan dipeptide is described on amylose stationary phase. The eluent used was CH 3 OH─CH 3 COONH 4 (10mM)─CH 3 CN (50: 40, 10) at 0.8‐mL/min flow, 230‐nm detection, 25‐minute run time, and 25°C ± 1°C temperature. The chiral phase was amylose [AmyCoat RP (15 cm × 0.46 cm × 5 micron)]. The magnitudes of the retention factors (k) were 2.71, 3.52, 5.11, and 7.75. The magnitudes of separation factor (α) were 1.19, 1.57, and 1.51 while the resolution factors (Rs) were 3.25, 14.84, and 15.76. The limits of detection and quantitation were of 2.5 to 5.4 and 12.8 to 27.5 μg/mL. The enantiomeric resolution is controlled by hydrogen, hydrophobic, π‐π, steric, etc interactions. The elution order of the enantiomer was supported by the modeling data. The described method is fast, reproducible, precise, and selective, which can be used successfully for evaluating the enantiomers of the reported dipeptide.