Affordable Access

Publisher Website

Biomimetic design of affinity peptide ligands for human IgG based on protein A-IgG complex

Authors
Journal
Biochemical Engineering Journal
1369-703X
Publisher
Elsevier
Publication Date
Volume
88
Identifiers
DOI: 10.1016/j.bej.2014.03.015
Keywords
  • Protein
  • Affinity
  • Adsorption
  • Chromatography
  • Purification
  • Molecular Simulation
Disciplines
  • Biology
  • Design

Abstract

Abstract Staphylococcal protein A (SpA) has been widely used as an affinity ligand for the purification of immunoglobulin G (IgG). Based on the affinity motif of SpA, we have herein developed a biomimetic design strategy for affinity peptide ligands of IgG. First, according to the distribution of the six hot spots of the SpA affinity motif determined previously, the number of residues that should be inserted into between the hot spots was determined. Cysteine was introduced as one of the middle inserted residues of the peptide for later immobilization. Then, amino acid location was performed to identify other amino acid residues for insertion, leading to the construction of a peptide library. The library was screened by using different molecular simulation protocols, resulting in the selection of 15 peptide candidates. Thereafter, molecular dynamics simulations were performed to validate the dynamics of the affinity interactions between the candidates and IgG, and 14 of them were found to keep high affinities. Finally, the affinity and specificity of the top one ligand FYWHCLDE were exemplified by protein chromatography and IgG purification. The results indicate that the design strategy was successful and the affinity peptide ligand for IgG is promising for application in antibody purifications.

There are no comments yet on this publication. Be the first to share your thoughts.