238000001042 affinity chromatography Methods 0.000 claims description 14.239000011159 matrix material Substances 0.000 claims description 18.108090001095 Immunoglobulin G Proteins 0.000 claims description 22.102000004851 Immunoglobulin G Human genes 0.000 claims description 22.DHMQDGOQFOQNFH-UHFFFAOYSA-N glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 28.238000004587 chromatography analysis Methods 0.000 claims description 34.239000007788 liquid Substances 0.000 claims abstract description 20.238000002360 preparation method Methods 0.000 claims abstract description 60.108091006437 Anion exchangers Proteins 0.000 claims abstract description 62.102000037197 Anion exchangers Human genes 0.000 claims abstract description 62.108090000623 proteins and genes Proteins 0.000 claims abstract description 176.102000004169 proteins and genes Human genes 0.000 claims abstract description 176.108090001123 antibodies Proteins 0.000 title claims description 30.102000004965 antibodies Human genes 0.000 title claims description 30.Publication of US20110166332A1 publication Critical patent/US20110166332A1/en Status Abandoned legal-status Critical Current Links Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.) Filing date Publication date Priority claimed from US19179008P external-priority Application filed by GE Healthcare Bio Sciences AB filed Critical GE Healthcare Bio Sciences AB Priority to US13/063,221 priority Critical patent/US20110166332A1/en Assigned to GE HEALTHCARE BIO-SCIENCES AB reassignment GE HEALTHCARE BIO-SCIENCES AB ASSIGNMENT OF ASSIGNORS INTEREST (SEE DOCUMENT FOR DETAILS). Original Assignee GE Healthcare Bio Sciences AB Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.) Gagnon Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Abandoned Application number US13/063,221 Inventor Peter S. Google Patents Enhanced antibody aggregate removal with capto adhere in the presence of protein-excluded zwitterionsĭownload PDF Info Publication number US20110166332A1 US20110166332A1 US13/063,221 US200913063221A US2011166332A1 US 20110166332 A1 US20110166332 A1 US 20110166332A1 US 200913063221 A US200913063221 A US 200913063221A US 2011166332 A1 US2011166332 A1 US 2011166332A1 Authority US United States Prior art keywords protein anion exchanger excluded multimodal anion column Prior art date Legal status (The legal status is an assumption and is not a legal conclusion. Google Patents US20110166332A1 - Enhanced antibody aggregate removal with capto adhere in the presence of protein-excluded zwitterions This study illustrates the role that wetting and dewetting play in modulating protein–ligand interactions.US20110166332A1 - Enhanced antibody aggregate removal with capto adhere in the presence of protein-excluded zwitterions To explore how these differences in dewetting affect protein–ligand interactions, we calculated the probability of each ligand binding to different types of residues on the protein surface and found that the probability of binding to a hydrophobic residue followed the same order as the dewetting behavior. We then explored how solvation was perturbed when the ligand was bound to the protein surface and found that the probability of the phenyl ring dewetting followed the order: Capto MMC > Prototype 4 > Nuvia cPrime. First, the solvation characteristics of each ligand were quantified via three metrics: average water density, fluctuations, and residence time. Our investigation focused on three chromatography ligands: Capto MMC, Nuvia cPrime, and Prototype 4, a structural variant of Nuvia cPrime. Here, we performed molecular dynamics simulations to explore how the ligand structure and geometry affect ligand–water interactions and how these differences in solution affect the nature of protein–ligand interactions. Recent studies have shown that selectivity in multimodal chromatographic separations is a function of the ligand structure and geometry. Multimodal chromatography is a powerful approach for purifying proteins that uses ligands containing multiple modes of interaction.
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