Thermodynamic benchmark study using Biacore technology

I. Navratilova; G.A. Papalia; R.L. Rich; D. Bedinger; S. Brophy; B. Condon; T. Deng; A.W. Emerick; H.W. Guan; T. Hayden; T. Heutmekers; B. Hoorelbeke; M.C. McCroskey; M.M. Murphy; T. Nakagawa; F. Parmeggiani; Q. Xiaochun; S. Rebe; T. Nenad; T. Tsang; M.B. Waddell; F.F. Zhang; S. Leavitt; D.G. Myszka

doi:10.1016/j.ab.2007.01.031

Thermodynamic benchmark study using Biacore technology

I. Navratilova, G.A. Papalia, R.L. Rich, D. Bedinger, S. Brophy, B. Condon, T. Deng, A.W. Emerick, H.W. Guan, T. Hayden, T. Heutmekers, B. Hoorelbeke, M.C. McCroskey, M.M. Murphy, T. Nakagawa, F. Parmeggiani, Q. Xiaochun, S. Rebe, T. Nenad, T. TsangM.B. Waddell, F.F. Zhang, S. Leavitt, D.G. Myszka

Research output: Contribution to journal › Article › Academic › peer-review

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Abstract

A total of 22 individuals participated in this benchmark study to characterize the thermodynamics of small-molecule inhibitor-enzyme interactions using Biacore instruments. Participants were provided with reagents (the enzyme carbonic anhydrase II, which was immobilized onto the sensor surface, and four sulfonamide-based inhibitors) and were instructed to collect response data from 6 to 36 °C. van't Hoff enthalpies and entropies were calculated from the temperature dependence of the binding constants. The equilibrium dissociation and thermodynamic constants determined from the Biacore analysis matched the values determined using isothermal titration calorimetry. These results demonstrate that immobilization of the enzyme onto the sensor surface did not alter the thermodynamics of these interactions. This benchmark study also provides insights into the opportunities and challenges in carrying out thermodynamic studies using optical biosensors

Original language	English
Pages (from-to)	67-77
Journal	Analytical Biochemistry
Volume	364
Issue number	1
DOIs	https://doi.org/10.1016/j.ab.2007.01.031
Publication status	Published - 2007

Keywords

equilibrium
binding
surface
users

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10.1016/j.ab.2007.01.031

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Navratilova, I., Papalia, G. A., Rich, R. L., Bedinger, D., Brophy, S., Condon, B., Deng, T., Emerick, A. W., Guan, H. W., Hayden, T., Heutmekers, T., Hoorelbeke, B., McCroskey, M. C., Murphy, M. M., Nakagawa, T., Parmeggiani, F., Xiaochun, Q., Rebe, S., Nenad, T., ... Myszka, D. G. (2007). Thermodynamic benchmark study using Biacore technology. Analytical Biochemistry, 364(1), 67-77. https://doi.org/10.1016/j.ab.2007.01.031

@article{36d1254819094c04ada97286f4476a8a,

title = "Thermodynamic benchmark study using Biacore technology",

abstract = "A total of 22 individuals participated in this benchmark study to characterize the thermodynamics of small-molecule inhibitor-enzyme interactions using Biacore instruments. Participants were provided with reagents (the enzyme carbonic anhydrase II, which was immobilized onto the sensor surface, and four sulfonamide-based inhibitors) and were instructed to collect response data from 6 to 36 °C. van't Hoff enthalpies and entropies were calculated from the temperature dependence of the binding constants. The equilibrium dissociation and thermodynamic constants determined from the Biacore analysis matched the values determined using isothermal titration calorimetry. These results demonstrate that immobilization of the enzyme onto the sensor surface did not alter the thermodynamics of these interactions. This benchmark study also provides insights into the opportunities and challenges in carrying out thermodynamic studies using optical biosensors",

keywords = "equilibrium, binding, surface, users",

author = "I. Navratilova and G.A. Papalia and R.L. Rich and D. Bedinger and S. Brophy and B. Condon and T. Deng and A.W. Emerick and H.W. Guan and T. Hayden and T. Heutmekers and B. Hoorelbeke and M.C. McCroskey and M.M. Murphy and T. Nakagawa and F. Parmeggiani and Q. Xiaochun and S. Rebe and T. Nenad and T. Tsang and M.B. Waddell and F.F. Zhang and S. Leavitt and D.G. Myszka",

year = "2007",

doi = "10.1016/j.ab.2007.01.031",

language = "English",

volume = "364",

pages = "67--77",

journal = "Analytical Biochemistry",

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number = "1",

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Navratilova, I, Papalia, GA, Rich, RL, Bedinger, D, Brophy, S, Condon, B, Deng, T, Emerick, AW, Guan, HW, Hayden, T, Heutmekers, T, Hoorelbeke, B, McCroskey, MC, Murphy, MM, Nakagawa, T, Parmeggiani, F, Xiaochun, Q, Rebe, S, Nenad, T, Tsang, T, Waddell, MB, Zhang, FF, Leavitt, S & Myszka, DG 2007, 'Thermodynamic benchmark study using Biacore technology', Analytical Biochemistry, vol. 364, no. 1, pp. 67-77. https://doi.org/10.1016/j.ab.2007.01.031

TY - JOUR

T1 - Thermodynamic benchmark study using Biacore technology

AU - Navratilova, I.

AU - Papalia, G.A.

AU - Rich, R.L.

AU - Bedinger, D.

AU - Brophy, S.

AU - Condon, B.

AU - Deng, T.

AU - Emerick, A.W.

AU - Guan, H.W.

AU - Hayden, T.

AU - Heutmekers, T.

AU - Hoorelbeke, B.

AU - McCroskey, M.C.

AU - Murphy, M.M.

AU - Nakagawa, T.

AU - Parmeggiani, F.

AU - Xiaochun, Q.

AU - Rebe, S.

AU - Nenad, T.

AU - Tsang, T.

AU - Waddell, M.B.

AU - Zhang, F.F.

AU - Leavitt, S.

AU - Myszka, D.G.

PY - 2007

Y1 - 2007

N2 - A total of 22 individuals participated in this benchmark study to characterize the thermodynamics of small-molecule inhibitor-enzyme interactions using Biacore instruments. Participants were provided with reagents (the enzyme carbonic anhydrase II, which was immobilized onto the sensor surface, and four sulfonamide-based inhibitors) and were instructed to collect response data from 6 to 36 °C. van't Hoff enthalpies and entropies were calculated from the temperature dependence of the binding constants. The equilibrium dissociation and thermodynamic constants determined from the Biacore analysis matched the values determined using isothermal titration calorimetry. These results demonstrate that immobilization of the enzyme onto the sensor surface did not alter the thermodynamics of these interactions. This benchmark study also provides insights into the opportunities and challenges in carrying out thermodynamic studies using optical biosensors

AB - A total of 22 individuals participated in this benchmark study to characterize the thermodynamics of small-molecule inhibitor-enzyme interactions using Biacore instruments. Participants were provided with reagents (the enzyme carbonic anhydrase II, which was immobilized onto the sensor surface, and four sulfonamide-based inhibitors) and were instructed to collect response data from 6 to 36 °C. van't Hoff enthalpies and entropies were calculated from the temperature dependence of the binding constants. The equilibrium dissociation and thermodynamic constants determined from the Biacore analysis matched the values determined using isothermal titration calorimetry. These results demonstrate that immobilization of the enzyme onto the sensor surface did not alter the thermodynamics of these interactions. This benchmark study also provides insights into the opportunities and challenges in carrying out thermodynamic studies using optical biosensors

KW - equilibrium

KW - binding

KW - surface

KW - users

U2 - 10.1016/j.ab.2007.01.031

DO - 10.1016/j.ab.2007.01.031

M3 - Article

SN - 0003-2697

VL - 364

SP - 67

EP - 77

JO - Analytical Biochemistry

JF - Analytical Biochemistry

IS - 1

ER -

Thermodynamic benchmark study using Biacore technology

Abstract

Keywords

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