Biosensor for integrin inhibition of mammalian cell adhesion and migration using micropatterned cell culture substrate and retroreflective optical signaling
Integrins are a family of transmembrane receptors that play a crucial role in cell adhesion and migration. Integrins can uniquely transduce biochemical signals bidirectionally across the membrane and physically link the cell-cell and cell-extracellular matrix (ECM) with ligand bonds. The arginyl-gly...
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            Elsevier
    
        2024-12-01
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| Series: | Sensing and Bio-Sensing Research | 
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2214180424000965 | 
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| author | Kyung Won Lee Eun Kyeong Yang Duc Long Nguyen Soo A Park Moon Suk Kim Jae-Ho Kim Min Young Lee Hyun C. Yoon  | 
    
| author_facet | Kyung Won Lee Eun Kyeong Yang Duc Long Nguyen Soo A Park Moon Suk Kim Jae-Ho Kim Min Young Lee Hyun C. Yoon  | 
    
| author_sort | Kyung Won Lee | 
    
| collection | DOAJ | 
    
| description | Integrins are a family of transmembrane receptors that play a crucial role in cell adhesion and migration. Integrins can uniquely transduce biochemical signals bidirectionally across the membrane and physically link the cell-cell and cell-extracellular matrix (ECM) with ligand bonds. The arginyl-glycyl-aspartic acid (RGD) peptide motif is present in the ECM as a minimal recognition sequence for integrins. To leverage this property in cell-based therapy, RGD variants, such as cyclic-type RGDfK (c(RGDfK)), which share a similar structure with RGD but exhibit a higher affinity for integrins, have been developed. However, because most evaluation methods for newly developed RGD variants focus on affinity strength, tools for cellular effects are required. In this study, we developed a new platform that integrates micropatterned three-dimensional cell culture substrates with a non-spectroscopic optical analysis system to quantitatively analyze the effects of RGD variants on cell adhesion and migration. The specially micropatterned substrate provides a cell adhesive and migration area to provide a restricted analysis area. Owing to the characteristics of retroreflective Janus particles (RJPs), a non-spectroscopic optical analysis system provides long-term stable optical verification properties and a simple optical setup. These techniques were integrated to quantitatively determine the integrin inhibitory effect of various concentrations of RGD variant. To demonstrate the efficacy of the developed cellular level RGD variant testing platform, the model cell line L929 fibroblast and model RGD variant c(RGDfK) were analyzed ranging from 0 to 10 μM. The results showed that the developed system could effectively and quantitatively analyze the effects of RGD variants on cells across various concentrations. | 
    
| format | Article | 
    
| id | doaj-art-e4fb7db3f96649cbadb3cd83d4630a56 | 
    
| institution | Kabale University | 
    
| issn | 2214-1804 | 
    
| language | English | 
    
| publishDate | 2024-12-01 | 
    
| publisher | Elsevier | 
    
| record_format | Article | 
    
| series | Sensing and Bio-Sensing Research | 
    
| spelling | doaj-art-e4fb7db3f96649cbadb3cd83d4630a562024-12-09T04:27:31ZengElsevierSensing and Bio-Sensing Research2214-18042024-12-0146100714Biosensor for integrin inhibition of mammalian cell adhesion and migration using micropatterned cell culture substrate and retroreflective optical signalingKyung Won Lee0Eun Kyeong Yang1Duc Long Nguyen2Soo A Park3Moon Suk Kim4Jae-Ho Kim5Min Young Lee6Hyun C. Yoon7Department of Molecular Science & Technology, Ajou University, Suwon 16499, Republic of KoreaDepartment of Molecular Science & Technology, Ajou University, Suwon 16499, Republic of KoreaDepartment of Molecular Science & Technology, Ajou University, Suwon 16499, Republic of KoreaDepartment of Molecular Science & Technology, Ajou University, Suwon 16499, Republic of KoreaDepartment of Molecular Science & Technology, Ajou University, Suwon 16499, Republic of KoreaDepartment of Molecular Science & Technology, Ajou University, Suwon 16499, Republic of Korea; Research Institute, ANK Corporation, Suwon 16522, Republic of KoreaDepartment of Otolaryngology-Head & Neck Surgery, College of Medicine, Dankook University, Cheonan 31116, Republic of KoreaDepartment of Molecular Science & Technology, Ajou University, Suwon 16499, Republic of Korea; Corresponding author.Integrins are a family of transmembrane receptors that play a crucial role in cell adhesion and migration. Integrins can uniquely transduce biochemical signals bidirectionally across the membrane and physically link the cell-cell and cell-extracellular matrix (ECM) with ligand bonds. The arginyl-glycyl-aspartic acid (RGD) peptide motif is present in the ECM as a minimal recognition sequence for integrins. To leverage this property in cell-based therapy, RGD variants, such as cyclic-type RGDfK (c(RGDfK)), which share a similar structure with RGD but exhibit a higher affinity for integrins, have been developed. However, because most evaluation methods for newly developed RGD variants focus on affinity strength, tools for cellular effects are required. In this study, we developed a new platform that integrates micropatterned three-dimensional cell culture substrates with a non-spectroscopic optical analysis system to quantitatively analyze the effects of RGD variants on cell adhesion and migration. The specially micropatterned substrate provides a cell adhesive and migration area to provide a restricted analysis area. Owing to the characteristics of retroreflective Janus particles (RJPs), a non-spectroscopic optical analysis system provides long-term stable optical verification properties and a simple optical setup. These techniques were integrated to quantitatively determine the integrin inhibitory effect of various concentrations of RGD variant. To demonstrate the efficacy of the developed cellular level RGD variant testing platform, the model cell line L929 fibroblast and model RGD variant c(RGDfK) were analyzed ranging from 0 to 10 μM. The results showed that the developed system could effectively and quantitatively analyze the effects of RGD variants on cells across various concentrations.http://www.sciencedirect.com/science/article/pii/S2214180424000965Integrin ligandRGD variants affinity assayMicropatterned 3D cell culture substrateRetroreflective Janus particlesNon-spectroscopic optical system | 
    
| spellingShingle | Kyung Won Lee Eun Kyeong Yang Duc Long Nguyen Soo A Park Moon Suk Kim Jae-Ho Kim Min Young Lee Hyun C. Yoon Biosensor for integrin inhibition of mammalian cell adhesion and migration using micropatterned cell culture substrate and retroreflective optical signaling Sensing and Bio-Sensing Research Integrin ligand RGD variants affinity assay Micropatterned 3D cell culture substrate Retroreflective Janus particles Non-spectroscopic optical system  | 
    
| title | Biosensor for integrin inhibition of mammalian cell adhesion and migration using micropatterned cell culture substrate and retroreflective optical signaling | 
    
| title_full | Biosensor for integrin inhibition of mammalian cell adhesion and migration using micropatterned cell culture substrate and retroreflective optical signaling | 
    
| title_fullStr | Biosensor for integrin inhibition of mammalian cell adhesion and migration using micropatterned cell culture substrate and retroreflective optical signaling | 
    
| title_full_unstemmed | Biosensor for integrin inhibition of mammalian cell adhesion and migration using micropatterned cell culture substrate and retroreflective optical signaling | 
    
| title_short | Biosensor for integrin inhibition of mammalian cell adhesion and migration using micropatterned cell culture substrate and retroreflective optical signaling | 
    
| title_sort | biosensor for integrin inhibition of mammalian cell adhesion and migration using micropatterned cell culture substrate and retroreflective optical signaling | 
    
| topic | Integrin ligand RGD variants affinity assay Micropatterned 3D cell culture substrate Retroreflective Janus particles Non-spectroscopic optical system  | 
    
| url | http://www.sciencedirect.com/science/article/pii/S2214180424000965 | 
    
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