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Comparison of weak affinity chromatography and surface plasmon resonance in determining affinity of small molecules
Linnaeus Univ, Dept Chem & Biomed Sci, SE-39182 Kalmar, Sweden.
Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
Linköping University, Department of Physics, Chemistry and Biology, Biotechnology. Linköping University, The Institute of Technology.
Linnaeus University, Sweden .
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2014 (English)In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 461, 57-59 p.Article in journal (Refereed) Published
Abstract [en]

In this study, we compared affinity data from surface plasmon resonance (SPR) and weak affinity chromatography (WAC), two established techniques for determination of weak affinity (mM-mu M) small molecule-protein interactions. In the current comparison, thrombin was used as target protein. In WAC the affinity constant (K-D) was determined from retention times, and in SPR it was determined by Langmuir isotherm fitting of steady-state responses. Results indicate a strong correlation between the two methods (R-2 = 0.995, P less than 0.0001).

Place, publisher, year, edition, pages
Elsevier Masson , 2014. Vol. 461, 57-59 p.
Keyword [en]
Affinity determination; Fragment-based drug discovery; Surface plasmon resonance; Thrombin; Weak affinity chromatography
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:liu:diva-110266DOI: 10.1016/j.ab.2014.05.023ISI: 000340077600009PubMedID: 24915639OAI: oai:DiVA.org:liu-110266DiVA: diva2:744058
Available from: 2014-09-05 Created: 2014-09-05 Last updated: 2017-12-05

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Bergström, GunnarMandenius, Carl-Fredrik

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