6533b820fe1ef96bd1279bf5
RESEARCH PRODUCT
New high-performance liquid chromatography-based methodology for monitoring the conformational transitions of self-associating hydrophobic peptides, incorporated into liposomes.
M.c. BañóConcepción AbadLorenzo Bracosubject
chemistry.chemical_classificationLiposomeChromatographyChemistryElutionVesicleOrganic ChemistryPhospholipidGramicidinPeptideGeneral MedicineBiochemistryHigh-performance liquid chromatographyAnalytical ChemistrySolventchemistry.chemical_compoundKineticsLiposomesGramicidinlipids (amino acids peptides and proteins)Spectrophotometry UltravioletPeptidesChromatography High Pressure Liquiddescription
A new high-performance size-exclusion chromatographic strategy is reported for the analysis of the hydrophobic self-associating peptide gramicidin A, incorporated into artificial phospholipid vesicles (liposomes). The method is based on the direct injection of a few microlitres of the gramicidin A-containing liposome suspension into the column, which is eluted with a non-polar solvent, such as tetrahydrofuran. The type and amount of information which can be derived from this methodology have been evaluated. Using this chromatographic approach, a correlation has been unambiguously shown to exist between the organization of the peptide in the vesicles and a number of variables involved in the method of preparation of liposomes. Finally, a gramicidin A conformational transition has been monitored in the phospholipid vesicles which proved to be dependent on the class of phospholipid present in the liposome.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1988-12-01 | Journal of chromatography |