Open-tubular electrochromatographic characterization of synthetic peptides.
Open-tubular electrochromatographic characterization of synthetic peptides.
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合成肽的开管电色谱表征。
DOI:
10.1002/elps.200405893
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发表时间:
2004
期刊:
影响因子:
2.9
通讯作者:
Hearn,MiltonTW
中科院分区:
文献类型:
--
作者:
Pesek,JosephJ;Matyska,MariaT;Dawson,GBrent;Chen,JennyI-Chen;Boysen,ReinhardI;Hearn,MiltonTW
The open‐tubular electrochromatographic (OT‐CEC) migration behavior of a series of peptides, based on a common structural feature, has been characterized using two different types of chemically modified etched capillaries. The organic moieties immobilized onto the capillary inner surface weren‐butylphenyl and cholesterol‐10‐undecenaoate, respectively. The structure‐migration behavior of this set of peptides has been studied at several pH values and with methanol at different concentrations as an organic solvent modifier of the buffer electrolyte composition. By comparing the structural properties of the peptides, such as their amino acid sequences, charge‐to‐mass ratios and intrinsic hydrophobicities to their migrational behavior, the relative contribution of electrophoretic and chromatographic mobility to the overall migration times, elution order, and selectivity has been determined. Moreover, the experimental data provide important insight into procedures that can be used to modulate the separation of peptides in OT‐CEC through variation of the composition of the electrolyte buffer as well asviathe properties of the bonded organic moiety.