Retention of Histidine-Containing Peptides on a Nickel Affinity Column

• Published in: Journal of chromatographic science Vol. 45; no. 4; pp. 207 - 211
• Main Authors: Kozlov, Igor A., Kermani, Bahram G., Melnyk, Peter C., Barker, David L., Zhao, Chanfeng, Hachmann, John P., Lebl, Michal
• Format: Journal Article
• Language: English
• Published: Niles, IL Oxford University Press 01-04-2007; Preston Publications
• Subjects: Amino Acid Sequence; Aminoacids, peptides. Hormones. Neuropeptides; Analytical chemistry; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Chemistry; Chromatographic methods and physical methods associated with chromatography; Chromatography, Affinity - instrumentation; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; Histidine - chemistry; Molecular Sequence Data; Nickel; Other chromatographic methods; Peptides - chemistry; Proteins; Affinity adsorbent; Ultraviolet detector; Analysis method; Nickel Complexes; Peptides; Affinity chromatography; Chromatographic retention; Immobilized metal affinity chromatography
• ISSN: 0021-9665; 1945-239X
• DOI: 10.1093/chromsci/45.4.207

The retention of histidine-containing peptides in immobilized metal-affinity chromatography is studied using several hundred modeled peptides. Retention is driven primarily by the number of histidine residues; however, the amino acid composition in the immediate vicinity plays a significant role. Specifically, the arginine and tryptophan content has to be taken into consideration. During the course of this study, an alternative tag that can be used similarly to a polyhistidine tag is discovered.