ISSN:
0899-0042
Keywords:
chirality
;
helicity
;
GC-stationary phase
;
conformations
;
1H-NMR-studies
;
molecular mechanics calculations
;
enantiomer separation
;
Chemistry
;
Organic Chemistry
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The manner of hydrogen-bonding to peptide selectors in enantiomer separation is examined with the help of a structural model. This model relies on a C3-symmetric trispeptide selector, which is stabilized by a network of distinct intramolecular hydrogen bonds. A combination of experimental and theoretical tools enables us to identify the lowest-energy conformation of the trispeptide selector and the sites of selector-substrate interactions. Experimental tools include temperature dependent 1H-NMR studies, 1D-NOE-measurements, and titration experiments, with the theoretical tools being EFF and CFF91 molecular mechanics calculations. The structural information deduced from these investigations is shown to bear on the enantioseparation of the corresponding chiral stationary phase towards derivatized amino acids. These observations, taken together, help to rationalize the mode of enantiomer-separation by amide phases as involving predominantly C7-hydrogen bonding sites. Chirality 10:396-404, 1998. © 1998 Wiley-Liss, Inc.
Additional Material:
5 Ill.
Type of Medium:
Electronic Resource
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