Surface Plasmon Resonance Studies of Protein Binding on Plasma Polymerized Di(ethylene glycol) Monovinyl Ether Films

Langmuir ◽  
2003 ◽  
Vol 19 (11) ◽  
pp. 4765-4770 ◽  
Author(s):  
Z. Zhang ◽  
B. Menges ◽  
R. B. Timmons ◽  
W. Knoll ◽  
R. Förch
2014 ◽  
Vol 10 ◽  
pp. 1672-1680 ◽  
Author(s):  
Silvia Bernardi ◽  
Paola Fezzardi ◽  
Gabriele Rispoli ◽  
Stefania E Sestito ◽  
Francesco Peri ◽  
...  

Four novel calix[4]arene-based glycoclusters were synthesized by conjugating the saccharide units to the macrocyclic scaffold using the CuAAC reaction and using long and hydrophilic ethylene glycol spacers. Initially, two galactosylcalix[4]arenes were prepared starting from saccharide units and calixarene cores which differ in the relative dispositions of the alkyne and azido groups. Once the most convenient synthetic pathway was selected, two further lactosylcalix[4]arenes were obtained, one in the cone, the other one in the 1,3-alternate structure. Preliminary studies of the interactions of these novel glycocalixarenes with galectin-3 were carried out by using a lectin-functionalized chip and surface plasmon resonance. These studies indicate a higher affinity of lactosyl- over galactosylcalixarenes. Furthermore, we confirmed that in case of this specific lectin binding the presentation of lactose units on a cone calixarene is highly preferred with respect to its isomeric form in the 1,3-alternate structure.


2011 ◽  
Vol 94 (4) ◽  
pp. 1217-1226 ◽  
Author(s):  
Pathik Vyas ◽  
Anthony A O'kane ◽  
E Ager ◽  
S Crooks ◽  
C Elliott ◽  
...  

Abstract A collaborative study was conducted on an inhibition-based protein-binding assay using the Biacore Q™ biosensor instrument and the Biacore Qflex™ Kit Vitamin B12 PI. The samples studied included infant formula, cereals, premixes, vitamin tablets, dietary supplements, and baby food. The collaborative study, which involved 11 laboratories, demonstrated that the assay showed an RSDr of 1.59–27.8 and HorRat values for reproducibility of 0.34–1.89 in samples with levels ranging from ppm to ppb. The assay studied is a label-free protein binding-based assay that uses the principle of surface plasmon resonance (SPR) to measure the interaction between vitamin B12 and a specifc binding protein. A Biacore Q biosensor uses this principle to detect binding directly at the surface of a sensor chip with a hydrophilic gold-dextran surface. The instrument passes a mixture of prepared sample extract and binding protein solution across a covalently immobilized vitamin B12 chip surface, and the response is given as free-binding protein as the mixture binds to the immobilized surface. This technique uses the specifcity and robustness of the protein-ligand interaction to allow minimal sample preparation and a wide range of matrixes to be analyzed rapidly. The reagents and accessories needed to perform this assay are provided as the ready-to-use format “Qflex Kit Vitamin B12 PI.” The method is intended for routine use in the quantitative determination of vitamin B12 (as cyanocobalamin) in a wide range of food products, dietary vitamin supplements, and multivitamin premixes.


2010 ◽  
Vol 1217 (13) ◽  
pp. 2032-2041 ◽  
Author(s):  
Tiago Vicente ◽  
José P.B. Mota ◽  
Cristina Peixoto ◽  
Paula M. Alves ◽  
Manuel J.T. Carrondo

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