Chiral Recognition of Amino Acids and Dipeptides by a Water-Soluble Zinc Porphyrin

A chiral water-soluble zinc porphyrin was optically resolved on a chiral HPLC column, and the binding of chiral amino acids and peptides to each of the enantiomers was examined spectrophotometrically in basic aqueous solution. The binding data apparently indicated that the zinc porphyrin has chiral...

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Published inInorganic chemistry Vol. 43; no. 4; pp. 1211 - 1213
Main Authors Imai, Hiroyasu, Munakata, Hiroki, Uemori, Yoshio, Sakura, Naoki
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 23.02.2004
Subjects
Amino Acids - chemistry
Chromatography, High Pressure Liquid
Circular Dichroism
Dipeptides - chemistry
Metalloporphyrins - chemistry
Molecular Conformation
Solubility
Solutions - chemistry
Spectrum Analysis
Stereoisomerism
Thermodynamics
Water - chemistry
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Summary:A chiral water-soluble zinc porphyrin was optically resolved on a chiral HPLC column, and the binding of chiral amino acids and peptides to each of the enantiomers was examined spectrophotometrically in basic aqueous solution. The binding data apparently indicated that the zinc porphyrin has chiral selectivity for amino acids and dipeptides. This was reasonably explained in terms of the triple cooperation of coordination, Coulomb, and steric interactions of the chiral amino carboxylates with the porphyrin. A compensatory relationship among the thermodynamic parameters for chiral recognition was also shown.
Bibliography:ObjectType-Article-1
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content type line 23
ISSN:0020-1669
1520-510X
DOI:10.1021/ic0302837