Evidence map›Paper›PMID 42460543›Full record

ArticleBiotechnology and bioengineering2026

Purification of Advanced Therapeutics by Flow-Through Pseudo-Affinity Chromatography: Bi-Specific mABs, Fc Fusion Proteins, and Adeno-Associated Viruses.

Wenning Chu, Eduardo Barbieri, Arianna Minzoni, Shriarjun Shastry, Jacob P LeBarre, Qingbo Shu, Taufika Williams, Xuanwen Li, Divya Chandra, Xuankuo Xu and 14 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biotechnology and bioengineering, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

24 authors.

Wenning ChuDepartment of Chemical and Biomolecular Engineering, NC State University, Raleigh, North Carolina, USA.ORCID https://orcid.org/0000-0002-6033-0963
Eduardo BarbieriDepartment of Chemical and Biomolecular Engineering, NC State University, Raleigh, North Carolina, USA.
Arianna MinzoniDepartment of Chemical and Biomolecular Engineering, NC State University, Raleigh, North Carolina, USA.ORCID https://orcid.org/0000-0002-4504-9567
Shriarjun ShastryDepartment of Chemical and Biomolecular Engineering, NC State University, Raleigh, North Carolina, USA.
Jacob P LeBarreDepartment of Chemical and Biomolecular Engineering, NC State University, Raleigh, North Carolina, USA.
Qingbo ShuMolecular Education, Technology, and Research Innovation Center (METRIC), NC State university, Raleigh, North Carolina, USA.
Taufika WilliamsMolecular Education, Technology, and Research Innovation Center (METRIC), NC State university, Raleigh, North Carolina, USA.
Xuanwen LiAnalytical Research & Development, Merck & Co., Rahway, New Jersey, USA.ORCID https://orcid.org/0000-0001-7548-583X
Divya ChandraProcess Research and Development, Merck & Co., Rahway, New Jersey, USA.ORCID https://orcid.org/0000-0002-3676-7209
Xuankuo XuBristol Myers Squibb, Devens, Massachusetts, USA.
Jerome BillGenentech Inc., 1 DNA Way, South San Francisco, California, USA.
David RoushRoush Biopharma Panacea, Colts Neck, New Jersey, USA.
Joseph TarisChromaGenix, Raleigh, North Carolina, USA.
Patrick GilbertChromaGenix, Raleigh, North Carolina, USA.
Andre KiesewetterMerck Life Science KGaA, Darmstadt, Germany.
Oliver RammoMerck Life Science KGaA, Darmstadt, Germany.
Michael SchulteMerck Life Science KGaA, Darmstadt, Germany.
Christopher MajorChromaGenix, Raleigh, North Carolina, USA.
Trina MouchahoirBiomolecular Measurement Division, National Institute of Standards and Technology, Gaithersburg, Maryland, USA.
Steven CramerDepartment of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York, USA.ORCID https://orcid.org/0000-0003-4993-0826
Cristiana BoiDepartment of Chemical and Biomolecular Engineering, NC State University, Raleigh, North Carolina, USA.
Ruben G CarbonellDepartment of Chemical and Biomolecular Engineering, NC State University, Raleigh, North Carolina, USA.
Abraham LenhoffNorth Carolina Viral Vector Initiative in Research and Learning (NC-VVIRAL), NC State University, Raleigh, North Carolina, USA.ORCID https://orcid.org/0000-0002-7831-219X
Stefano MenegattiDepartment of Chemical and Biomolecular Engineering, NC State University, Raleigh, North Carolina, USA.ORCID https://orcid.org/0000-0001-5633-434X

Funding

FDA HHS R01 FD007481FDA HHS R01FD007481National Institute for Innovation in Manufacturing Biopharmaceuticals PC3.1-119National Institute for Innovation in Manufacturing Biopharmaceuticals PC5.2-133National Institute for Innovation in Manufacturing Biopharmaceuticals PC8.1-135North Carolina Viral Vector Initiative in Research and Learning (NC-VVIRAL)Novo Foundation NNF19SA0035474
6 · The paper itself

Abstract

Modern biopharmaceutical manufacturing requires purification platforms capable of processing structurally and functionally diverse products while addressing the challenge of removing persistent and high-risk host cell proteins (HCPs). Current purification processes utilize adsorbents that operate in bind-and-elute mode, which limits productivity, and often struggle to remove critical impurities. Addressing these limitations, our team developed a flow-through pseudo-affinity chromatography platform that utilizes size-exclusion resins (Monomix Core 500) functionalized with mixed-mode peptide ligands (AviGuard) to remove process-related impurities while maximizing productivity and product integrity. This study evaluates this technology across three therapeutic modalities: two bi-specific monoclonal antibodies (bsAbs) and an Fc-fusion protein from Chinese hamster ovary (CHO) cell culture fluids, and adeno-associated virus serotypes 2 and 9 (AAV2 and AAV9) from HEK293 cell lysates. For the CHO-derived proteins, the platform comprised a pre-capture step with LigaGuard-Monomix Core 500 resin (LGMC500), a Protein A-based capture step, and a polishing step using a single-use size-exclusion mixed-mode (SEMM) resin. This configuration achieved global product yields exceeding 70%, final product pool concentration > 15 mg/mL, monomeric purity ~99%, and excellent cumulative HCP clearance (LRV > 4.5) to residual levels of 60-165 ng/mL (4-11 ppm). For AAV purification, the process utilized a mixed-bed adsorbent comprising dextran-coated charcoal and LGMC500 for removing HCPs, cell metabolites, and media components, followed by a capture step using either CaptureSelect AAVX resin or Natrix CH membranes. The optimization of the charcoal-to-resin volume ratio (1:3) and load volume (~ 10

Indexed as

Antibodies, MonoclonalChromatography, AffinityDependovirusImmunoglobulin Fc FragmentsRecombinant Fusion ProteinsAnimalsCHO CellsCricetinaeCricetulusHEK293 CellsHumansAntibodies, MonoclonalImmunoglobulin Fc FragmentsRecombinant Fusion Proteinsadeno‐associated virusbi‐specific antibodiesFc‐fusion proteinsflow‐through chromatographyhost cell proteins

Identifiers

PMID42460543
PMCPMC13665647

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.