Characterization of Receptor Binding Affinity for Vascular Endothelial Growth Factor with Interferometric Imaging Sensor.

Age-related macular degeneration (AMD) Interferometric Reflectance Imaging Sensor (IRIS) Vascular Endothelial Growth Factor (VEGF) aflibercept anti-VEGF drug bevacizumab

Journal

Biosensors
ISSN: 2079-6374
Titre abrégé: Biosensors (Basel)
Pays: Switzerland
ID NLM: 101609191

Informations de publication

Date de publication:
24 Jun 2024
Historique:
received: 02 05 2024
revised: 18 06 2024
accepted: 20 06 2024
medline: 26 7 2024
pubmed: 26 7 2024
entrez: 26 7 2024
Statut: epublish

Résumé

Wet Age-related macular degeneration (AMD) is the leading cause of vision loss in industrialized nations, often resulting in blindness. Biologics, therapeutic agents derived from biological sources, have been effective in AMD, albeit at a high cost. Due to the high cost of AMD treatment, it is critical to determine the binding affinity of biologics to ensure their efficacy and make quantitative comparisons between different drugs. This study evaluates the in vitro VEGF binding affinity of two drugs used for treating wet AMD, monoclonal antibody-based bevacizumab and fusion protein-based aflibercept, performing quantitative binding measurements on an Interferometric Reflectance Imaging Sensor (IRIS) system. Both biologics can inhibit Vascular Endothelial Growth Factor (VEGF). For comparison, the therapeutic molecules were immobilized on to the same support in a microarray format, and their real-time binding interactions with recombinant human VEGF (rhVEGF) were measured using an IRIS. The results indicated that aflibercept exhibited a higher binding affinity to VEGF than bevacizumab, consistent with previous studies using ELISA and SPR. The IRIS system's innovative and cost-effective features, such as silicon-based semiconductor chips for enhanced signal detection and multiplexed analysis capability, offer new prospects in sensor technologies. These attributes make IRISs a promising tool for future applications in the development of therapeutic agents, specifically biologics.

Identifiants

pubmed: 39056591
pii: bios14070315
doi: 10.3390/bios14070315
pii:
doi:

Substances chimiques

Vascular Endothelial Growth Factor A 0
Bevacizumab 2S9ZZM9Q9V
Receptors, Vascular Endothelial Growth Factor EC 2.7.10.1
aflibercept 15C2VL427D
VEGFA protein, human 0
Recombinant Fusion Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Auteurs

Nese Lortlar Ünlü (N)

Faculty of Medicine, Histology and Embryology, Atlas University, 34408 İstanbul, Turkey.
Photonics Center, Department of Biomedical Engineering, Boston University, Boston, MA 02215, USA.

Monireh Bakhshpour-Yucel (M)

Department of Chemistry, Faculty of Arts and Science, Bursa Uludag University, 16059 Bursa, Turkey.
Photonics Center, Department of Electrical Engineering, Boston University, Boston, MA 02215, USA.

Elisa Chiodi (E)

Photonics Center, Department of Electrical Engineering, Boston University, Boston, MA 02215, USA.

Sinem Diken-Gür (S)

Photonics Center, Department of Electrical Engineering, Boston University, Boston, MA 02215, USA.
Department of Biology, Hacettepe University, 06800 Ankara, Turkey.

Sinan Emre (S)

Batigoz Eye Health Branch Center, 35210 Izmir, Turkey.

M Selim Ünlü (MS)

Photonics Center, Department of Biomedical Engineering, Boston University, Boston, MA 02215, USA.
Photonics Center, Department of Electrical Engineering, Boston University, Boston, MA 02215, USA.

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Classifications MeSH