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Comparative analysis of 10 small molecules binding to carbonic anhydrase II by different investigators using Biacore technology

  1. Author:
    Papalia, G. A.
    Leavitt, S.
    Bynum, M. A.
    Katsamba, P. S.
    Wilton, R.
    Qiu, H. W.
    Steukers, M.
    Wang, S. M.
    Bindu, L.
    Phogat, S.
    Giannetti, A. M.
    Ryan, T. E.
    Pudlak, V. A.
    Matusiewicz, K.
    Michelson, K. M.
    Nowakowski, A.
    Pham-Baginski, A.
    Brooks, J.
    Tieman, B. C.
    Bruce, B. D.
    Vaughn, M.
    Baksh, M.
    Cho, Y. H.
    De Wit, M.
    Smets, A.
    Vandersmissen, J.
    Michiels, L.
    Myszka, D. G.

  2. Author Address

    Univ Utah, Ctr Biomol Interact Anal, Sch Med, Salt Lake City, UT 84132 USA. Gilead Sci, Foster City, CA 94404 USA. Agilent Technol, Palo Alto, CA 94304 USA. Argonne Natl Lab, Argonne, IL 60439 USA. Genzyme Corp, Framingham, MA 01701 USA. Dyaxsa, B-4000 Liege 1, Belgium. Georgia State Univ, Atlanta, GA 30302 USA. NCI, Frederick, MD 21702 USA. NIAID, Bethesda, MD 20892 USA. Reichert Analyt Instruments, Depew, NY 14043 USA. Adamed, PL-05152 Czosnow, Poland. Amgen Inc, Thousand Oaks, CA 91320 USA. diaDexus, San Francisco, CA 94080 USA. Wyeth, Andover, MA 01810 USA. Wyeth, Cambridge, MA 02140 USA. Abbott Labs, Abbott Pk, IL 60064 USA. Univ Tennessee, Knoxville, TN 37996 USA. Univ Calif Berkeley, Berkeley, CA 94720 USA. Human Genome Sci, Rockville, MD 20850 USA. Tibotec, B-2800 Mechelen, Belgium.;Myszka, DG, Univ Utah, Ctr Biomol Interact Anal, Sch Med, Salt Lake City, UT 84132 USA.;dmyszka@cores.utah.edu
    1. Year: 2006
    2. Date: Dec
  2. Journal: Analytical Biochemistry
    1. 359
    2. 1
    3. Pages: 94-105
  4. Type of Article: Article
  5. ISSN: 0003-2697
  1. Abstract:

    In this benchmark study, 26 investigators were asked to characterize the kinetics and affinities of 10 sulfonamide inhibitors binding to the enzyme carbonic anhydrase II using Biacore optical biosensors. A majority of the participants collected data that could be fit to a 1:1 interaction model, but a subset of the data sets obtained from some instruments were of poor quality. The experimental errors in the k(a), k(d), and K-D parameters determined for each of the compounds averaged 34, 24, and 37%, respectively. As expected, the greatest variation in the reported constants was observed for compounds with exceptionally weak affinity and/or fast association rates. The binding constants determined using the biosensor correlated well with solution-based titration calorimetry measurements. The results of this study provide insight into the challenges, as well as the level of experimental variation, that one would expect to observe when using Biacore technology for small molecule analyses. (c) 2006 Elsevier Inc. All rights reserved.

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External Sources

  1. View Full Text
  2. DOI: 10.1016/j.ab.2006.08.021
  3. View record in Web of Science®
  4. WOS: 000242108900012

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