The role of ion-pairing in peak deformations in overloaded reversed-phase chromatography of peptides.
The paper reports a study on the role of ion-pairing behind peak deformations, e.g. peak splitting and even peak disappearance, during the elution of a peptide at highly overloaded conditions in reversed-phase chromatography. Deformation of component peaks is not uncommon in chromatography. There are reports which discuss their occurrence, but mostly at analytical scale, while their occurrence is quite common also in the preparative scale, as in the case discussed in this work. This paper first describes the conditions leading to peak splitting and peak disappearance of an industrial peptide, then explains the plausible reasons behind such behaviour, and finally with experimental analysis demonstrates the role of ion-pairing in causing such behaviour.
Tarafder
Abhijit
A
ETH Zurich, Institute for Chemical and Bioengineering, 10 Wolfgang Pauli Strasse, 8093 Zurich, Switzerland.
Aumann
Lars
L
Morbidelli
Massimo
M
D000097:Acetonitriles; D000327:Adsorption; D000595:Amino Acid Sequence; D002116:Calcitonin / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D056148:Chromatography, Reverse-Phase / Q000379:methods*; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D010756:Phosphoric Acids
D000097:Acetonitriles; D010455:Peptides; D010756:Phosphoric Acids; D002116:Calcitonin; C030242:phosphoric acid; C032159:acetonitrile