title: Algorithms for the quantitative validation of chiral properties of peptides.
abstract: Complexation with Cu(II) ion in strong aqueous base, combined with visible range circular dichroism detection, were used to quantitatively differentiate among the L-enantiomers of the GG, GA, GY, AG, AA, AY, YG, YA, and YY dipeptides and the D-enantiomer of GA. Using ellipticity data at all (n = 1500) wavelengths in the measured spectra, and two novel data reduction procedures, quantitative determinations were made of the compositions of binary mixtures. For mixtures made with the L-GA and D-GA enantiomers, the accuracy of the measured enantiomeric purities was better than 0.17 % over the 1-48 % range for the minor component. The method has considerable potential for use in quality control of peptide and protein biotechnological drug forms.
authors.affiliation: Department of Chemistry, Oklahoma State University, Stillwater, Oklahoma 74078-0447, USA.
authors.forename: N
authors.initials: N
authors.lastname: Purdie
authors.forename: D W
authors.initials: DW
authors.lastname: Province
mesh_terms: D000465:Algorithms; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry; D018360:Crystallography, X-Ray; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012996:Solutions; D013237:Stereoisomerism
chemical_list: D010455:Peptides; D012996:Solutions; D003300:Copper