Surface Plasmon Resonance Identifies High-Affinity Binding of l-DOPA to Siderocalin/Lipocalin-2 through Iron–Siderophore Action: Implications for Parkinson’s Disease Treatment

Author(s):  
Sammy Alhassen ◽  
Mehmet Senel ◽  
Amal Alachkar
2012 ◽  
Vol 84 (14) ◽  
pp. 6031-6039 ◽  
Author(s):  
Nathan J. Wittenberg ◽  
Hyungsoon Im ◽  
Xiaohua Xu ◽  
Bharath Wootla ◽  
Jens Watzlawik ◽  
...  

2016 ◽  
Vol 161 (1) ◽  
pp. 37-43 ◽  
Author(s):  
Natsuki Fukuda ◽  
Yoshiaki Suwa ◽  
Makiyo Uchida ◽  
Yoshihiro Kobashigawa ◽  
Hideshi Yokoyama ◽  
...  

The Analyst ◽  
2019 ◽  
Vol 144 (15) ◽  
pp. 4526-4533 ◽  
Author(s):  
Pan Li ◽  
Meihong Ge ◽  
Chentai Cao ◽  
Dongyue Lin ◽  
Liangbao Yang

Fe3O4/Au composites demonstrated a coupled enhanced mechanism allowing for sensitive detection of dopamine in complicated specimens subjected to simple pretreatment.


Blood ◽  
2011 ◽  
Vol 117 (12) ◽  
pp. 3460-3468 ◽  
Author(s):  
Kerrie A. Smith ◽  
Penelope J. Adamson ◽  
Richard J. Pease ◽  
Jane M. Brown ◽  
Anthony J. Balmforth ◽  
...  

Abstract Fibrinogen αC residues 242-424 have been shown to have a major regulatory role in the activation of factor XIII-A2B2 (FXIII-A2B2); however, the interactions underpinning this enhancing effect have not been determined. Here, we have characterized the binding of recombinant (r)FXIII-A subunit and FXIII-A2B2 with fibrin(ogen) and fibrin αC residues 233-425. Using recombinant truncations of the fibrin αC region 233-425 and surface plasmon resonance, we found that activated rFXIII-A bound αC 233-425 (Kd of 2.35 ± 0.09μM) which was further localized to αC 389-403. Site-directed mutagenesis of this region highlighted Glu396 as a key residue for binding of activated rFXIII-A. The interaction was specific for activated rFXIII-A and depended on the calcium-induced conformational change known to occur in rFXIII-A during activation. Furthermore, nonactivated FXIII-A2B2, thrombin-cleaved FXIII-A2B2, and activated FXIII-A2B2 each bound fibrin(ogen) and specifically αC region 371-425 with high affinity (Kd < 35nM and Kd < 31nM, respectively), showing for the first time the potential involvement of the αC region in binding to FXIII-A2B2. These results suggest that in addition to fibrinogen γ′ chain binding, the fibrin αC region also provides a platform for the binding of FXIII-A2B2 and FXIII-A subunit.


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Marten Beeg ◽  
Cesare Burti ◽  
Eleonora Allocati ◽  
Clorinda Ciafardini ◽  
Rita Banzi ◽  
...  

AbstractMeasurements of serum concentrations of therapeutic antibodies and anti-drug antibodies (ADA) can support clinical decisions for the management of non-responders, optimizing the therapy. In the present study we compared the results obtained by classical ELISA and a recently proposed surface plasmon resonance (SPR)-based immunoassay, in 76 patients receiving infliximab for inflammatory bowel diseases. The two methods indicated very similar serum concentrations of the drug, but there were striking differences as regards ADA. All the sera showing ADA by ELISA (14) also showed ADA by SPR, but the absolute amounts were different, being 7–490 times higher with SPR, with no correlation. Eight patients showed ADA only with SPR, and these ADA had significantly faster dissociation rate constants than those detectable by both SPR and ELISA. The underestimation, or the lack of detection, of ADA by ELISA is likely to reflect the long incubation steps which favor dissociation of the patient’s low-affinity ADA, while the commercial, high-affinity anti-infliximab antibodies used for the calibration curve do not dissociate. This problem is less important with SPR, which monitors binding in real time. The possibility offered by SPR to detect ADA in patients otherwise considered ADA-negative by ELISA could have important implications for clinicians.


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