Investigation of Interaction of Vaccinia Virus Complement Control Protein and Curcumin with Complement Components C3 and C3b Using Quartz Crystal Microbalance with Dissipation Monitoring Technology
Amod P. Kulkarnia, Philippa J. Randalla, Krishna Murthyb, Lauriston A. Kellawaya, Girish J. Kotwal*, c
Identifiers and Pagination:Year: 2010
First Page: 9
Last Page: 21
Publisher ID: TOBIOCJ-4-9
Article History:Received Date: 10/11/2009
Revision Received Date: 7/12/2009
Acceptance Date: 14/12/2009
Electronic publication date: 27/1/2010
Collection year: 2010
open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http: //creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.
C3 and C3b, the components central to the complement activation, also play a damaging role in several inflammatory disorders. Vaccinia virus complement control protein (VCP) and curcumin (Cur) are natural compounds with different biological origins reported to regulate complement activation. However, both VCP and Cur have not been investigated for their interaction with the third component (C3) prior to it being converted to its activated form (C3b). These two compounds have also not been compared to each other with respect to their interactions with C3 and C3b. Quartz crystal microbalance with dissipation monitoring (QCM-D) is a novel technology used to study the interaction of biomolecules. This technology was applied to characterize the interactions of VCP, Cur and appropriate controls with the key complement components. Cur as well as VCP showed binding to both C3 and to C3b, Cur however bound to C3b to a lesser extent.