A controlled immobilization of His-tagged estrogen receptor hERa: Comparison study between the kinetics and morphology


A controlled immobilization of His-tagged estrogen receptor hERa: Comparison study between the kinetics and morphology

Cherkouk, C.; Rebohle, L.; Gerlach, T.; Kunze, G.; Lenk, J.; Ou, X.; Pietzsch, J.; Skorupa, W.

A specific immobilization of macrobiomolecules on chip arrays is essential in order to increase the efficiency of biosensors as well as for the improvement of protein single studies. A comparison between a specific immobilization, like on nickel-nitrilotriacetic acid (Ni-NTA) matrix, and a covalent immobilization, like on amino self-assembling monolayers (SAMs), was investigated by using surface plasmon resonance (SPR). Whereas the number of the covalently immobilized estrogen receptors hER is higher than those of the specifically immobilized receptors, the affinity constant KD, using β-Estradiol as an analyte, is much higher in the case of the specific immobilization. This fact has been demonstrated by means of atomic force microscopy (AFM) and scanning electron microscopy (SEM), respectively. The morphology of the covalent and specific immobilization of the His-tagged binding domain of the estrogen receptor (hERa-LBD-His10) confirms the SPR kinetics study.

Keywords: Estrogen receptor; Ni-NTA; His-tagged; SPR; AFM; SEM

  • Lecture (Conference)
    E-MRS 2012 SPRING MEETING, 14.-18.05.2012, Strasbourg, France

Permalink: https://www.hzdr.de/publications/Publ-17159
Publ.-Id: 17159