AFM study of cytochrome CYP102A1 oligomeric state

Yuri D. Ivanov; Natalia S. Bukharina; Pavel A. Frantsuzov; Tatyana O. Pleshakova; Sergey L. Kanashenko; Natalia V. Medvedeva; Viktoriya V. Argentova; Viktor G. Zgoda; Andrew W. Munro; Alexander I. Archakov

doi:10.1039/C2SM07333A

AFM study of cytochrome CYP102A1 oligomeric state†

Yuri D. Ivanov,^a Natalia S. Bukharina,*^a Pavel A. Frantsuzov,^a Tatyana O. Pleshakova,^a Sergey L. Kanashenko,^a Natalia V. Medvedeva,^a Viktoriya V. Argentova,^a Viktor G. Zgoda,^a Andrew W. Munro^b and Alexander I. Archakov^a

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^a Institute of Biomedical Chemistry of Russian Academy of Biomedical Sciences, Pogodinskaya St. 10, Moscow, Russia
E-mail: natalie_buharina@list.ru
Fax: +7 499 2450857
Tel: +7 499 2463761

^b The University of Manchester, Carys Bannister Building, Dover St., Manchester, UK
E-mail: andrew.munro@manchester.ac.uk
Tel: +44 0 1613065151

Abstract

Atomic force microscopy (AFM) study of the oligomeric state of CYP102A1 was carried out in three different environmental conditions – liquid, air and vacuum. It was shown that usage of a standard probe with a radius of curvature of 10 nm allowed determination of the monomers-to-oligomers ratio, α ≈ 0.5 : 0.5, in these three media, but it wasn't possible to estimate the oligomerization degree more precisely. Application of a supersharp probe with a radius of curvature of 2 nm made it possible not only to obtain data on the ratio of monomers-to-oligomers but also to obtain the approximate ratio between dimers, trimers and tetramers 0.3 : 0.1 : 0.1, but only in vacuum.

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AFM study of cytochrome CYP102A1 oligomeric state†

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