An experimental check of backscattering interferometry

被引：4

作者：

Baksh, Michael M. ^{[1
]}

Finn, M. G. ^{[1
]}

机构：

[1] Georgia Inst Technol, Sch Chem & Biochem, Atlanta, GA 30306 USA

来源：

SENSORS AND ACTUATORS B-CHEMICAL | 2017年 / 243卷

关键词：

Backscattering interferometry; Label-free; Binding constants; Protein-ligand interactions; Experimental methods; LABEL-FREE; PROTEIN INTERACTIONS; BINDING; INDEX; QUANTIFICATION; PROBE;

D O I：

10.1016/j.snb.2016.12.055

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Backscattering interferometry (BSI) was used to determine the association constants for four wellknown biomolecular interactions: protein A+IgG, trypsin + antitrypsin, trypsin + p-aminobenzamidine, and antithrombin + heparin. Each gave well-defined binding curves and Kd values in close agreement with published findings obtained using other techniques. These results stand in direct contrast to the claims in a 2015 publication in this journal (Discussion of "Back Scattering Interferometry revisited a theoretical and experimental investigation" Jorgensen, T.M.; Jepsen, S.T.; Sorensen, H.S.; di Gennaro,A.K.; Kristensen, S.R. Sensors and Actuators B 2015, 220,1328-1337, doi: 10.1016/j.snb.2015.06.121), thus invalidating the claim that BSI is unable to make measurements of this kind. The experimental details are discussed, and several potential sources of error in the previous publication are identified. No comments are made here on the discussion of the theoretical aspects of the BSI technique. (C) 2016 Elsevier B.V. All rights reserved.

引用

页码：977 / 981

页数：5

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