Issue 41, 2016
From the journal:

RSC Advances

Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling†

Jovana Trbojević Ivić,a   Aleksandra Dimitrijević,b   Nenad Milosavić,*c   Dejan Bezbradica,d   Branko J. Drakulić,e   Marija Gavrović Jankulović,f   Marija Pavlović,g   Helene Rogniauxg  and  Dušan Veličkovićf  

* Corresponding authors

a Innovation Center, Faculty of Chemistry, University of Belgrade, 11000 Belgrade, Serbia

b Department of Molecular Biology and Biochemistry, University of California Irvine, 92697 Irvine, California, USA

c Division of Experimental Therapeutics, Department of Medicine, Columbia University, 10032 New York, New York, USA
E-mail: nm2729@cumc.columbia.edu

d Department of Biochemical Engineering and Biotechnology, Faculty of Technology and Metallurgy, 11000 Belgrade, Serbia

e Department of Chemistry, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Belgrade, Serbia

f Department of Biochemistry, Faculty of Chemistry, 11000 Belgrade, Serbia

g INRA, UR1268, Biopolymers Interactions Assembles, 44316 Nantes, France

Abstract

Hydroxyapatite (HAP), a calcium-phosphate bioactive ceramic, is actively employed in medical and separation sciences. Although different classes of biomacromolecules interact with this material, interactions with proteins are the most important, since they directly affect the biocompatibility of the carrier and it's industrial application. In the presented work, we thoroughly investigate and elucidate the interaction mechanism between Candida rugosa lipase (CRL) upon it's immobilization on HAP, since this immobilized enzyme showed advanced catalytic properties in previous studies. Applying elution and protein modification strategies we concluded that Ca-chelation of HAP's C-site and CRL's –COOH groups is the most probable interacting mechanism. A proteomics approach revealed that this chelation is conserved throughout all CRL isoforms, while results of molecular modelling led us to propose the involvement of a specific region of the protein surface and side chains in interactions with HAP.

Graphical abstract: Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling

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Article information

DOI
https://doi.org/10.1039/C6RA07521E
Article type
Paper
Submitted
22 Mar 2016
Accepted
29 Mar 2016
First published
01 Apr 2016

RSC Adv., 2016,6, 34818-34824

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Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling

J. T. Ivić, A. Dimitrijević, N. Milosavić, D. Bezbradica, B. J. Drakulić, M. G. Jankulović, M. Pavlović, H. Rogniaux and D. Veličković, RSC Adv., 2016, 6, 34818 DOI: 10.1039/C6RA07521E

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