Review on biomimetic affinity chromatography with short peptide ligands and its application to protein purification

Fang, Yu-Ming; Lin, Dong‐Qiang; Yao, Shan‐Jing

doi:10.1016/j.chroma.2018.07.082

Cited by 61 publications

(27 citation statements)

References 106 publications

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“…Figure 2B showed this resin had a stable binding ability to BSA at pH 5.0–8.0 compared to the hIgG that might be caused by the isoelectric points of hIgG (pH 6.5) and BSA (pH 4.8) [16]. Moreover, compared to the non‐grafted Ac‐YFRH‐4FF resin (pH 7.0, Q m = 80 mg hIgG/g resin, K d = 7.00 mg/mL), Ac‐YFRH‐XL resin showed much lower K d (pH 7.0, Q m = 81 mg hIgG/g resin, K d = 0.13 mg/mL), which indicated stronger binding ability of dextran‐grafted resin due to its “chain transfer” power [26]. Further, the highest binding capacity could reach to 133 mg/g with low K d (0.03 mg/mL) at pH 8.9, which even showed better binding ability to non‐grafted resin with the highest binding capacity of 100.5 mg/g [12], indicating the potential advantages of grafted resin for antibody purification.…”

Section: Resultsmentioning

confidence: 99%

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A novel dextran‐grafted tetrapeptide resin for antibody purification

Fang

Zhu

Lin

et al. 2020

J of Separation Science

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Short peptide biomimetic affinity chromatography as a novel antibody separation chromatography is a potential alternative to protein A chromatography. However, if directly attaching ligand to matrix, the adsorption capacity and mass transfer rate would be affected by pore blockage and steric effect. Grafting resin is an effective method to solve this problem by using polymer as a bridge between matrix and ligand. In this work, a novel resin was prepared by grafting a tetrapeptide to the dextran-grafted matrix. Then, the adsorption properties for human immunoglobin G and BSA were determined. The results showed the saturation adsorption capacity could reach to 133 mg/g resin at pH 8.9 with a significantly low dissociation constant (0.03 mg/mL). The influence of flow rates to dynamic binding capacity of this resin was less than that of the non-grafted resin. The separation performance of the resin showed monoclonal antibody could be well isolated from the Chinese hamster ovary culture supernatant at pH 9.0 with the purity of 93.0% and yield of 84.7% by one step. Overall, this resin could achieve higher binding capacity by the possible of gaining higher ligand density, indicating its potential significance for separation in larger scale systems.

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Section: Resultsmentioning

confidence: 99%

“…The results demonstrate the selectivity of the resin to hIgG could be increased by adjusting the NaCl concentration. Moreover, compared to the non‐grafted resin ( K d = 2.1–7.0 mg/mL) [12], Ac‐YFRH‐XL resin showed much lower K d (0.17–0.91 mg/mL) values, which indicates higher binding ability of the polymer‐grafted resin [26].…”

Section: Resultsmentioning

confidence: 99%

A novel dextran‐grafted tetrapeptide resin for antibody purification

Fang

Zhu

Lin

et al. 2020

J of Separation Science

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“…As an import part of biomimetic ligands, short peptide ligands have raised increasing interest in the recent years. 26 Peptide ligands have advantages of low immunogenicity, easy synthesis, easy modification, higher surface density, and more amenability for engineering at the molecular level. 27 In view of a series of excellent peptide ligand properties, affinity adsorbents with peptide ligands have been developed as the main technology for target protein separation and purification.…”

Section: Introductionmentioning

confidence: 99%

“…27 In view of a series of excellent peptide ligand properties, affinity adsorbents with peptide ligands have been developed as the main technology for target protein separation and purification. 26 …”

Section: Introductionmentioning

confidence: 99%

<p>Integrated System for Purification and Assembly of PCV Cap Nano Vaccine Based on Targeting Peptide Ligand</p>

Wang

Hao

et al. 2020

IJN

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Purpose The vaccine design has shifted from attenuated or inactivated whole pathogen vaccines to more pure and defined subunit vaccines. The purification of antigen proteins, especially the precise display of antigen regions, has become a key step affecting the effectiveness of subunit vaccines. Materials and Methods This work presents the application of molecular docking for a peptide ligand designed for PCV2 Cap purification and assembly in one step. Based on the PCV2 Cap protein affinity peptide (L11-DYWWQSWE), the amino terminal of PCV2 Cap was covalently coupled with the polylactic acid–glycolic acid copolymer (PLGA) carboxyl terminal through the EDC/NHS method. Results The PLGA had an average diameter of 106 nm. The average diameter increased to 122 nm after the PCV2 Cap protein conjugation, and the Zeta potential shifted from −13.7 mV to −9.6 mV, indicating that the PCV2 Cap protein stably binds to the PLGA. Compared with the free PCV2 Cap protein group, the neutralizing antibody titer was significantly increased on the 14th day after the PLGA-Cap immunization (P < 0.05). The neutralizing antibody level was extremely significant on the 28th day (P < 0.001). The CCK-8 analysis showed that PLGA-Cap had an obvious cytotoxic effect on RAW264.7 cells at the PLGA nanoparticle concentration up to 200 μg/mL but had no obvious cytotoxic effect on DC2.4 cells. Compared with the Cap protein group, the antigen-presenting cells had a stronger antigen uptake capacity and a higher fluorescence in the PLGA-Cap group. The immune effect showed that the level of the neutralizing antibody produced by this structure is much better than that of purified protein and helps improve the immune system response. Conclusion This technology provides a potential new perspective for the rapid enrichment of the antigen protein with the affinity peptide ligand.

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“…Small peptide ligands have been highlighted over the past few decades on account of their particular advantages, such as less cost, little immunogenic responses and more stable physicochemical properties ( 1 , 2 ). Especially, peptide ligands’ chemical structures are highly compatible with those of the target proteins ( 3 ).…”

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confidence: 99%

OUP accepted manuscript

Wang

et al. 2020

Database

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DPL ( http://www.peptide-ligand.cn/ ) is a comprehensive database of peptide ligand (DPL). DPL1.0 holds 1044 peptide ligand entries and provides references for the study of the polypeptide platform. The data were collected from PubMed-NCBI, PDB, APD3, CAMPR3, etc. The lengths of the base sequences are varied from 3 to78. DPL database has 923 linear peptides and 88 cyclic peptides. The functions of peptides collected by DPL are very wide. It includes 540 entries of antiviral peptides (including SARS-CoV-2), 55 entries of signal peptides, 48 entries of protease inhibitors, 45 entries of anti-hypertension, 37 entries of anticancer peptides, etc. There are 270 different kinds of peptide targets. All peptides in DPL have clear binding targets. Most of the peptides and receptors have 3D structures experimentally verified or predicted by CYCLOPS, I-TASSER and SWISS-MODEL. With the rapid development of the COVID-2019 epidemic, this database also collects the research progress of peptides against coronavirus. In conclusion, DPL is a unique resource, which allows users easily to explore the targets, different structures as well as properties of peptides.

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Review on biomimetic affinity chromatography with short peptide ligands and its application to protein purification

Cited by 61 publications

References 106 publications

A novel dextran‐grafted tetrapeptide resin for antibody purification

A novel dextran‐grafted tetrapeptide resin for antibody purification

<p>Integrated System for Purification and Assembly of PCV Cap Nano Vaccine Based on Targeting Peptide Ligand</p>

OUP accepted manuscript

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