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Peer-reviewedCC BYRSC advances

Heparinization of anodized aluminum oxide (AAO) membranes for affinity separations of biocolloids.

  • Kayla E Daugherty1
  • Logan D Martin1
  • Mara Leach-Baughman1
  • Kearstin L Edmonds2
  • Rebecca E Dutch2
  • Malgorzata Chwatko1
  • Stephen E Rankin1
  • Barbara L Knutson1
  1. 1University of Kentucky, Department of Chemical & Materials Engineering Lexington KY 40406-0046 USA [email protected] [email protected].
  2. 2University of Kentucky, Department of Molecular and Cellular Biochemistry Lexington KY 40506 USA.
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Abstract

Affinity membranes are developed by the immobilization of heparin onto anodized aluminum oxide (AAO) supports via amine grafting followed by amide coupling. Optimized procedures give heparinized AAO (HEP-AAO) membranes with a stable layer of 0.832-1.33 mg heparin per m² pore area in 224 nm diameter pores. Following the heparinization of the membrane, the bioavailability of heparin is demonstrated through the capture and release of fibroblast growth factor 2 (FGF2), a protein for which heparin acts as a ligand. The capping of unreacted amines using citraconic anhydride reduces nonspecific protein binding without loss of heparin activity. The pore accessibility of colloidal particles is confirmed through the electrostatically-driven binding and release of 20 nm fluorescent amine-grafted silica nanoparticles, which are used as a model system to investigate the capture and release of biocolloids. Application of heparinized AAO membranes for the affinity capture and release of adeno associated virus 2 (AAV-2) is demonstrated in tangential flow filtration. Preliminary results for the affinity capture of AAV-2 pre-filtered culture medium capture significant AAV2 with negligible retention of host protein and DNA, paving a path for further optimization of viral vector purification.

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Cite

BibTeXRIS
BibTeX
@article{daugherty2026heparinization,
  title = {{Heparinization of anodized aluminum oxide (AAO) membranes for affinity separations of biocolloids.}},
  author = {Kayla E Daugherty and Logan D Martin and Mara Leach-Baughman and Kearstin L Edmonds and Rebecca E Dutch and Malgorzata Chwatko and Stephen E Rankin and Barbara L Knutson},
  journal = {RSC advances},
  year = {2026},
  month = oct,
  doi = {10.1039/d6ra07687d},
  url = {https://europepmc.org/article/MED/42903969},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Heparinization of anodized aluminum oxide (AAO) membranes for affinity separations of biocolloids.
AU  - Kayla E Daugherty
AU  - Logan D Martin
AU  - Mara Leach-Baughman
AU  - Kearstin L Edmonds
AU  - Rebecca E Dutch
AU  - Malgorzata Chwatko
AU  - Stephen E Rankin
AU  - Barbara L Knutson
PY  - 2026
DA  - 2026/10/20
JO  - RSC advances
DO  - 10.1039/d6ra07687d
UR  - https://europepmc.org/article/MED/42903969
AB  - Affinity membranes are developed by the immobilization of heparin onto anodized aluminum oxide (AAO) supports via amine grafting followed by amide coupling. Optimized procedures give heparinized AAO (HEP-AAO) membranes with a stable layer of 0.832-1.33 mg heparin per m² pore area in 224 nm diameter pores. Following the heparinization of the membrane, the bioavailability of heparin is demonstrated through the capture and release of fibroblast growth factor 2 (FGF2), a protein for which heparin acts as a ligand. The capping of unreacted amines using citraconic anhydride reduces nonspecific protein binding without loss of heparin activity. The pore accessibility of colloidal particles is confirmed through the electrostatically-driven binding and release of 20 nm fluorescent amine-grafted silica nanoparticles, which are used as a model system to investigate the capture and release of biocolloids. Application of heparinized AAO membranes for the affinity capture and release of adeno associated virus 2 (AAV-2) is demonstrated in tangential flow filtration. Preliminary results for the affinity capture of AAV-2 pre-filtered culture medium capture significant AAV2 with negligible retention of host protein and DNA, paving a path for further optimization of viral vector purification.
SN  - 2046-2069
ER  -