Exploring the Interaction of Biotinylated FcGamma RI and IgG1 Monoclonal Antibodies on Streptavidin-Coated Plasmonic Sensor Chips for Label-Free VEGF Detection
Vascular endothelial growth factor (VEGF) is a critical angiogenesis biomarker associated with various pathological conditions, including cancer. This study leverages pre-biotinylated FcγRI interactions with IgG1-type monoclonal antibodies to develop a sensitive VEGF detection method. Utilizing surf...
Saved in:
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2024-12-01
|
| Series: | Biosensors |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2079-6374/14/12/634 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850240526377287680 |
|---|---|
| author | Soodeh Salimi Khaligh Fahd Khalid-Salako Hasan Kurt Meral Yüce |
| author_facet | Soodeh Salimi Khaligh Fahd Khalid-Salako Hasan Kurt Meral Yüce |
| author_sort | Soodeh Salimi Khaligh |
| collection | DOAJ |
| description | Vascular endothelial growth factor (VEGF) is a critical angiogenesis biomarker associated with various pathological conditions, including cancer. This study leverages pre-biotinylated FcγRI interactions with IgG1-type monoclonal antibodies to develop a sensitive VEGF detection method. Utilizing surface plasmon resonance (SPR) technology, we characterized the binding dynamics of immobilized biotinylated FcγRI to an IgG1-type antibody, Bevacizumab (AVT), through kinetic studies and investigated suitable conditions for sensor surface regeneration. Subsequently, we characterized the binding of FcγRI-captured AVT to VEGF, calculating kinetic constants and binding affinity. A calibration curve was established to analyze the VEGF quantification capacity and accuracy of the biosensor, computing the limits of blank, detection, and quantification at a 95% confidence interval. Additionally, the specificity of the biosensor for VEGF over other protein analytes was assessed. This innovative biomimetic approach enabled FcγRI-mediated site-specific AVT capture, establishing a stable and reusable platform for detecting and accurately quantifying VEGF. The results indicate the effectiveness of the plasmonic sensor platform for VEGF detection, making it suitable for research applications and, potentially, clinical diagnostics. Utilizing FcγRI-IgG1 antibody binding, this study highlights the industrial and clinical value of advanced biosensing technologies, offering insights to enhance therapeutic monitoring and improve outcomes in anti-VEGF therapies. |
| format | Article |
| id | doaj-art-9fea955feddd44e599a49843952a950e |
| institution | OA Journals |
| issn | 2079-6374 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biosensors |
| spelling | doaj-art-9fea955feddd44e599a49843952a950e2025-08-20T02:00:51ZengMDPI AGBiosensors2079-63742024-12-01141263410.3390/bios14120634Exploring the Interaction of Biotinylated FcGamma RI and IgG1 Monoclonal Antibodies on Streptavidin-Coated Plasmonic Sensor Chips for Label-Free VEGF DetectionSoodeh Salimi Khaligh0Fahd Khalid-Salako1Hasan Kurt2Meral Yüce3SUNUM Nanotechnology Research and Application Centre, Sabanci University, Istanbul 34956, TürkiyeSUNUM Nanotechnology Research and Application Centre, Sabanci University, Istanbul 34956, TürkiyeDepartment of Bioengineering, Royal School of Mines, Imperial College London, London SW7 2AZ, UKSUNUM Nanotechnology Research and Application Centre, Sabanci University, Istanbul 34956, TürkiyeVascular endothelial growth factor (VEGF) is a critical angiogenesis biomarker associated with various pathological conditions, including cancer. This study leverages pre-biotinylated FcγRI interactions with IgG1-type monoclonal antibodies to develop a sensitive VEGF detection method. Utilizing surface plasmon resonance (SPR) technology, we characterized the binding dynamics of immobilized biotinylated FcγRI to an IgG1-type antibody, Bevacizumab (AVT), through kinetic studies and investigated suitable conditions for sensor surface regeneration. Subsequently, we characterized the binding of FcγRI-captured AVT to VEGF, calculating kinetic constants and binding affinity. A calibration curve was established to analyze the VEGF quantification capacity and accuracy of the biosensor, computing the limits of blank, detection, and quantification at a 95% confidence interval. Additionally, the specificity of the biosensor for VEGF over other protein analytes was assessed. This innovative biomimetic approach enabled FcγRI-mediated site-specific AVT capture, establishing a stable and reusable platform for detecting and accurately quantifying VEGF. The results indicate the effectiveness of the plasmonic sensor platform for VEGF detection, making it suitable for research applications and, potentially, clinical diagnostics. Utilizing FcγRI-IgG1 antibody binding, this study highlights the industrial and clinical value of advanced biosensing technologies, offering insights to enhance therapeutic monitoring and improve outcomes in anti-VEGF therapies.https://www.mdpi.com/2079-6374/14/12/634VEGF biosensorFcγRImonoclonal antibodiessurface plasmon resonance (SPR)biosensing technology |
| spellingShingle | Soodeh Salimi Khaligh Fahd Khalid-Salako Hasan Kurt Meral Yüce Exploring the Interaction of Biotinylated FcGamma RI and IgG1 Monoclonal Antibodies on Streptavidin-Coated Plasmonic Sensor Chips for Label-Free VEGF Detection Biosensors VEGF biosensor FcγRI monoclonal antibodies surface plasmon resonance (SPR) biosensing technology |
| title | Exploring the Interaction of Biotinylated FcGamma RI and IgG1 Monoclonal Antibodies on Streptavidin-Coated Plasmonic Sensor Chips for Label-Free VEGF Detection |
| title_full | Exploring the Interaction of Biotinylated FcGamma RI and IgG1 Monoclonal Antibodies on Streptavidin-Coated Plasmonic Sensor Chips for Label-Free VEGF Detection |
| title_fullStr | Exploring the Interaction of Biotinylated FcGamma RI and IgG1 Monoclonal Antibodies on Streptavidin-Coated Plasmonic Sensor Chips for Label-Free VEGF Detection |
| title_full_unstemmed | Exploring the Interaction of Biotinylated FcGamma RI and IgG1 Monoclonal Antibodies on Streptavidin-Coated Plasmonic Sensor Chips for Label-Free VEGF Detection |
| title_short | Exploring the Interaction of Biotinylated FcGamma RI and IgG1 Monoclonal Antibodies on Streptavidin-Coated Plasmonic Sensor Chips for Label-Free VEGF Detection |
| title_sort | exploring the interaction of biotinylated fcgamma ri and igg1 monoclonal antibodies on streptavidin coated plasmonic sensor chips for label free vegf detection |
| topic | VEGF biosensor FcγRI monoclonal antibodies surface plasmon resonance (SPR) biosensing technology |
| url | https://www.mdpi.com/2079-6374/14/12/634 |
| work_keys_str_mv | AT soodehsalimikhaligh exploringtheinteractionofbiotinylatedfcgammariandigg1monoclonalantibodiesonstreptavidincoatedplasmonicsensorchipsforlabelfreevegfdetection AT fahdkhalidsalako exploringtheinteractionofbiotinylatedfcgammariandigg1monoclonalantibodiesonstreptavidincoatedplasmonicsensorchipsforlabelfreevegfdetection AT hasankurt exploringtheinteractionofbiotinylatedfcgammariandigg1monoclonalantibodiesonstreptavidincoatedplasmonicsensorchipsforlabelfreevegfdetection AT meralyuce exploringtheinteractionofbiotinylatedfcgammariandigg1monoclonalantibodiesonstreptavidincoatedplasmonicsensorchipsforlabelfreevegfdetection |