A new paper on the selection and design of a peptide ligand for the separation of human erythropoietin has been published in the Journal of Chromatography A. The publication focuses on work primarily performed by William Kish during his time in the lab as a doctoral student.
The work tells about the search for cyclic ligands that bind erythropoietin with higher specificity, and includes information about how the authors had to combat the peptide library’s propensity to produce sequences that were primarily hydrophobic in nature. The use of in-silico docking informed the study, a tool the lab is currently using and developing to make our processes and searches better tuned and better understood.
The paper is currently available online – check it out!
Citation and link: William S Kish, Hiroyuki Sachi, Amith D Naik, Matthew K Roach, Benjamin G Bobay, Robert K Blackburn, Stefano Menegatti, Ruben G Carbonell. Design, selection, and development of cyclic peptide ligands for human erythropoietin. J. Chrom. A. 2017.
Keywords: Erythropoietin; Cyclic peptide ligands; Ligand screening; Affinity chromatography; Affinity maturation; In-silico docking
Journal of Chromatography A image came from the J. Chrom. A description on Elsevier.
Hannah Reese went to the 253rd American Chemical Society meeting in San Fransisco. She presented some of her work in the lab on the separation of IgG isoforms to the BIOT division of the meeting. She would like to thank our collaborator, Allen Hirsh from Cryobiophysica, for providing the piSEP buffer and gradient maker system. Way to go, Hannah!