Analysis of the carbohydrate binding specificity of the mushroom Pleurotus ostreatus lectin by surface plasmon resonance

2005 ◽  
Vol 336 (1) ◽  
pp. 87-93 ◽  
Author(s):  
Yuka Kobayashi ◽  
Hiroko Nakamura ◽  
Takehiko Sekiguchi ◽  
Ryo Takanami ◽  
Takeomi Murata ◽  
...  
1999 ◽  
Vol 274 (2) ◽  
pp. 203-210 ◽  
Author(s):  
Simon R. Haseley ◽  
Philippe Talaga ◽  
Johannis P. Kamerling ◽  
Johannes F.G. Vliegenthart

Materials ◽  
2018 ◽  
Vol 11 (12) ◽  
pp. 2348 ◽  
Author(s):  
Katrin Niegelhell ◽  
Thomas Ganner ◽  
Harald Plank ◽  
Evelyn Jantscher-Krenn ◽  
Stefan Spirk

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.


2005 ◽  
Vol 876 ◽  
Author(s):  
Chanda Yonzon ◽  
Richard P. Van Duyne

AbstractThis work encompasses a comparative analysis of the properties of two optical biosensor platforms: (1) the propagating surface plasmon resonance (SPR) sensor based on a planar, thin film gold surface and (2) the localized surface plasmon resonance (LSPR) sensor based on surface confined Ag nanoparticles fabricated by nanosphere lithography. The binding of Concanavalin A (ConA) to mannose-functionalized self-assembled monolayers (SAMs) is chosen to illustrate the similarities and the differences of these sensors. A comprehensive set of non-specific binding studies demonstrate that the single transduction mechanism is due to the specific binding of ConA to the mannose-functionalized surface. Finally, an elementary (2x1) multiplexed version of a LSPR carbohydrate sensing chip to probe the simultaneous binding of ConA to mannose and galactose-functionalized SAMs is also demonstrated.


The Analyst ◽  
2008 ◽  
Vol 133 (2) ◽  
pp. 206-212 ◽  
Author(s):  
Chantal Gondran ◽  
Marie-Pierre Dubois ◽  
Sébastien Fort ◽  
Serge Cosnier ◽  
Sabine Szunerits

2012 ◽  
Vol 350 ◽  
pp. 49-54 ◽  
Author(s):  
Sachiko Nakamura-Tsuruta ◽  
Michiko Yasuda ◽  
Toshiyuki Nakamura ◽  
Eri Shinoda ◽  
Takashi Furuyashiki ◽  
...  

2007 ◽  
Vol 282 (46) ◽  
pp. 33681-33690 ◽  
Author(s):  
Momoko Kimura ◽  
Tae Yamamoto ◽  
Jianyong Zhang ◽  
Ken Itoh ◽  
Motoki Kyo ◽  
...  

Nrf2-small Maf heterodimer activates the transcription of many cytoprotective genes through the antioxidant response element and serves as a key factor in xenobiotic and oxidative stress responses. Our surface plasmon resonance-microarray binding analysis revealed that both Nrf2-MafG heterodimer and MafG homodimer bind to the consensus Maf recognition element with high affinity but bind differentially to the suboptimal binding sequences degenerated from the consensus. We examined the molecular basis distinguishing the binding profile of Nrf2-MafG heterodimer from that of MafG homodimer and found that the Ala-502 residue in the basic region of Nrf2 is a critical determinant of its binding specificity. In Maf proteins, a tyrosine resides in the position corresponding to Ala-502 in Nrf2. We prepared a mutant Nrf2 molecule in which Ala-502 was replaced with tyrosine. In surface plasmon resonance-microarray analysis, heterodimer of Nrf2(A502Y) and MafG displayed a binding specificity similar to that of MafG homodimer. The target genes activated by mutant Nrf2(A502Y)-small Maf heterodimer were largely different, albeit with some overlap, from those activated by wild-type Nrf2-small Maf, indicating that the array of target genes regulated by Nrf2-small Maf heterodimer differs substantially from that regulated by Maf homodimer in vivo. These results suggest that the distinct DNA binding profile of Nrf2-Maf heterodimer is biologically significant for Nrf2 to function as a key regulator of cytoprotective genes. Our contention is supported that the differential DNA binding specificity between Maf homodimers and Nrf2-Maf heterodimers establishes the differential gene regulation by these dimer-forming transcription factors.


2020 ◽  
pp. 44-49
Author(s):  
I. N. Pavlov

Two optical methods, namely surface plasmon resonance imaging and frustrated total internal reflection, are described in the paper in terms of comparing their sensitivity to change of refractive index of a thin boundary layer of an investigated medium. It is shown that, despite the fact that the theoretically calculated sensitivity is higher for the frustrated total internal reflection method, and the fact that usually in practice the surface plasmon resonance method, on the contrary, is considered more sensitive, under the same experimental conditions both methods show a similar result.


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