Ion-interaction CZE: the presence of high concentrations of ion-pairing reagents demonstrates the complex mechanisms involved in peptide separations.

Ion-interaction CZE: the presence of high concentrations of ion-pairing reagents demonstrates the complex mechanisms involved in peptide separations. Research Abstract Details 

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Ion-interaction CZE: the presence of high concentrations of ion-pairing reagents demonstrates the complex mechanisms involved in peptide separations. Abstract Text:

Traian V Popa,Colin T Mant,Robert S Hodges,

We have furthered our understanding of the separative mechanism of a novel CE approach, termed ion-interaction CZE (II-CZE), developed in our laboratory for the resolution of mixtures of cationic peptides. Thus, II-CZE and RP-HPLC were applied to the separation of peptides differing by a single amino acid substitution in 10- and 12-residue synthetic model peptide sequences. Substitutions differed by a wide range of properties or side-chain type (e.g., alkyl side-chains, polar side-chains, etc.) at the substitution site. When carried out in high concentrations (400 mM) of pentafluoropropionic acid (PFPA), II-CZE separated peptides in order of increasing hydrophobicity when the substituted side-chains were of a similar type; when II-CZE was applied to the mixtures of peptides with substitutions of side-chains that differed in the type of functional group, there was no longer a correlation of electrophoretic mobility in II-CZE with relative peptide hydrophobicity, suggesting that a third factor is involved in the separative mechanism beyond charge and hydrophobicity. Interestingly, the hydrophobic PFPA- anion is best for separating peptides that differ in hydrophobicity with hydrophobic side-chains but high concentrations of the hydrophilic H2PO4- anion are best when separating peptides that differ in polar side-chains relative to hydrophobic side-chains. We speculate that differential hydration/dehydration properties of various side-chains in the peptide and the hydration/dehydration properties of the hydrophilic/hydrophobic anions as well as the electrostatic attractions between the peptide and the anions in solution all play a critical role in these solution-based effects.

Ion-interaction CZE: the presence of high concentrations of ion-pairing reagents demonstrates the complex mechanisms involved in peptide separations. Publishing Authors By Initials

TV Popa,CT Mant,RS Hodges,

For similar investigative techniques: epidemiologic methods: epidemiologic research design: reproducibility of results research abstracts see: investigative techniques: epidemiologic methods: epidemiologic research design: reproducibility of results research

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Ion-interaction CZE: the presence of high concentrations of ion-pairing reagents demonstrates the complex mechanisms involved in peptide separations. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Electrophoresis

VOLUME: 28

Page Numbers: 2181-90

Journal Abbreviation: Electrophoresis

ISSN: 0173-0835

DAY: 3

MONTH: Jul

YEAR: 2007

Ion-interaction CZE: the presence of high concentrations of ion-pairing reagents demonstrates the complex mechanisms involved in peptide separations. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8204476

Ion-interaction CZE: the presence of high concentrations of ion-pairing reagents demonstrates the complex mechanisms involved in peptide separations. Keywords Mesh Terms:

KEYWORDS: Reproducibility of Results

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Ion-interaction CZE: the presence of high concentrations of ion-pairing reagents demonstrates the complex mechanisms involved in peptide separations. Information

Substance Name: Peptides

Registry Number: 0

Grant and Affiliation Information for Ion-interaction CZE: the presence of high concentrations of ion-pairing reagents demonstrates the complex mechanisms involved in peptide separations.

AFFILIATION: Department of Biochemistry and Molecular Genetics, University of Colorado at Denver and Health Sciences Center, Aurora, CO 80045, USA.

Country: Germany

AGENCY: United States NIGMS

GRANT: R01GM 61855

ACRONYM: GM

MEDLINETA: Electrophoresis

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