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Updated: Jun 4, 2026
Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis
Published on: October 15, 2021
Removal of intact β2-microglobulin at neutral ph by using seed-conjugated polymer beads prepared with
Sungsoo Kang1, Jee Eun Yang, Jehoon Kim
1School of Chemical and Biological Engineering, Seoul National University, Seoul 151-744, Korea.
Abstract:
Removal of β2-microglobulin (β2M) from the blood of patients suffering from kidney dysfunction is crucial to protect those individuals from getting the diseased state of dialysis-related amyloidosis. By harnessing the nucleation-dependent fibrillation process of amyloidogenesis, a β2M removal strategy has been proposed by preparing seed-conjugated polymer beads and assimilating soluble β2M to the fibrils on the surface at neutral pH. A novel peptide segment of β2M ranging from residue 58 to residue 67 (Lys-Asp-Trp-Ser-Phe-Tyr-Leu-Leu-Tyr-Tyr), which was capable of being fibrillated at neutral pH was isolated. Charge interaction between the positive N-terminal lysine and the negative C-terminal α-carboxylic group was demonstrated to be critical for the molecular self-assembly leading to the peptide fibril formation by favoring β-sheet conformation. Because the peptide fibrils were successful to seed intact β2M at neutral pH, the fibrils were immobilized on polymer beads of HiCore resins, and the resulting seed-conjugated beads were used to accrete intact β2M in the form of fibrils elongated on the bead surface. Its efficiency of the β2M removal was improved by placing the seed-immobilized beads in the middle of a continuous flow of the β2M-containing solution as practiced in the blood circulation during the hemodialysis. Therefore, this β2M removal system is suggested to exhibit high specificity, high binding capacity, and cost-effectiveness appropriate for eventual clinical application to remove β2M from the blood of renal failure patients.
Insights
This study developed a novel method to remove beta2-microglobulin (β2M) using seeded polymer beads, effectively preventing dialysis-related amyloidosis in kidney dysfunction patients.
Area of Science:
- Biomedical Engineering
- Protein Chemistry
- Renal Medicine
Background:
- Dialysis-related amyloidosis is a risk for kidney dysfunction patients due to beta2-microglobulin (β2M) buildup.
- Current methods for β2M removal are insufficient, necessitating innovative strategies.
Purpose of the Study:
- To develop an efficient and specific method for removing β2M from blood.
- To create a system for preventing dialysis-related amyloidosis.
Main Methods:
- Isolated a novel β2M peptide segment (residues 58-67) that self-assembles into fibrils at neutral pH.
- Immobilized these peptide fibrils onto HiCore polymer beads to create seed-conjugated beads.
- Utilized the seed-conjugated beads in a continuous flow system to capture and fibrillate soluble β2M.
Main Results:
- Demonstrated that charge interactions are critical for peptide fibril formation and β-sheet conformation.
- Successfully seeded intact β2M onto immobilized peptide fibrils at neutral pH.
- Achieved efficient β2M removal using the continuous flow system with seed-conjugated beads.
Conclusions:
- The developed β2M removal system shows high specificity and binding capacity.
- The system is cost-effective and suitable for clinical application in hemodialysis.
- This approach offers a promising strategy to mitigate dialysis-related amyloidosis.
