Detailed evaluation of protein adsorption on alumina surface through surface plasmon resonance phenomenon

2012 ◽  
Vol 258 (24) ◽  
pp. 9526-9530 ◽  
Author(s):  
Hiroki Akasaka ◽  
Miyuki Konishi ◽  
Naoki Gawazawa ◽  
Shigeo Ohshio ◽  
Ikumi Toda ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Protein Adsorption ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Resonance Phenomenon ◽  
Alumina Surface ◽  
Detailed Evaluation

scholarly journals Lectins at Interfaces—An Atomic Force Microscopy and Multi-Parameter-Surface Plasmon Resonance Study

Materials ◽  
2018 ◽  
Vol 11 (12) ◽  
pp. 2348 ◽  
Author(s):  
Katrin Niegelhell ◽  
Thomas Ganner ◽  
Harald Plank ◽  
Evelyn Jantscher-Krenn ◽  
Stefan Spirk
Keyword(s):  
Atomic Force Microscopy ◽  
Surface Plasmon Resonance ◽  
Protein Adsorption ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Resonance Spectroscopy ◽  
Carbohydrate Binding ◽  
Force Microscopy ◽  
Atomic Force ◽  
Slow Kinetics

Lectins are a diverse class of carbohydrate binding proteins with pivotal roles in cell communication and signaling in many (patho)physiologic processes in the human body, making them promising targets in drug development, for instance, in cancer or infectious diseases. Other applications of lectins employ their ability to recognize specific glycan epitopes in biosensors and glycan microarrays. While a lot of research has focused on lectin interaction with specific carbohydrates, the interaction potential of lectins with different types of surfaces has not been addressed extensively. Here, we screen the interaction of two specific plant lectins, Concanavalin A and Ulex Europaeus Agglutinin-I with different nanoscopic thin films. As a control, the same experiments were performed with Bovine Serum Albumin, a widely used marker for non-specific protein adsorption. In order to test the preferred type of interaction during adsorption, hydrophobic, hydrophilic and charged polymer films were explored, such as polystyrene, cellulose, N,-N,-N-trimethylchitosan chloride and gold, and characterized in terms of wettability, surface free energy, zeta potential and morphology. Atomic force microscopy images of surfaces after protein adsorption correlated very well with the observed mass of adsorbed protein. Surface plasmon resonance spectroscopy studies revealed low adsorbed amounts and slow kinetics for all of the investigated proteins for hydrophilic surfaces, making those resistant to non-specific interactions. As a consequence, they may serve as favorable supports for biosensors, since the use of blocking agents is not necessary.

Influence of surface roughness on surface plasmon resonance phenomenon of gold film

2016 ◽  
Vol 14 (4) ◽  
pp. 042401-42403 ◽  
Author(s):  
Zhitao Yang Zhitao Yang ◽  
Changjian Liu Changjian Liu ◽  
Yachen Gao Yachen Gao ◽  
Jiyu Wang Jiyu Wang ◽  
and Wenlong Yang and Wenlong Yang
Keyword(s):  
Surface Roughness ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Gold Film ◽  
Resonance Phenomenon
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