RT Book, Section
T1 Chemokine Detection Using Receptors Immobilized on an SPRSensor Surface
A1 Rodríguez Frade, José Miguel
A1 Martínez Muñoz, Laura
A1 Villares, Ricardo
A1 Cascio, Graciela
A1 Lucas, Pilar
A1 Pérez Gomáriz, Rosa María
A1 Mellado, Mario
AB Chemokines and their receptors take part in many physiological and pathological processes, and their dysregulated expression is linked to chronic inflammatory and autoimmune diseases, immunodeficiencies, and cancer. The chemokine receptors, members of the G protein-coupled receptor family, are integral membrane proteins, with seven-transmembrane domains that bind the chemokines and transmit signals through GTP-binding proteins. Many assays used to study the structure, conformation, or activation mechanism of these receptors are based on ligand-binding measurement,as are techniques to detect new agonists and antagonists that modulate chemokine function. Such methods require labeling of the chemokine and/or its receptor, whichcan alter their binding characteristics. Surface plasmon resonance (SPR) is a powerful technique for analysis of the interaction between immobilized receptors and ligands in solution, in real time, and without labeling. SPR measurements nonetheless require expression and purification steps that can alter the conformation, stability, and function of the chemokine and/or the chemokine receptor. In this review, we focus on distinct methods to immobilize chemokine receptors on the surface of an optical biosensor. We expose the advantages and disadvantages of different protocols used and describe in detail the method to retain viral particles as receptor carriers that can be used for SPR determinations.
PB Elsevier
SN 9780128021712 (Hardcover)  9780128021958 (ebook)
SN 0076-6879, ESSN: 1557-7988
YR 2016
FD 2016
LK https://hdl.handle.net/20.500.14352/24914
UL https://hdl.handle.net/20.500.14352/24914
LA eng
NO Comunidad de Madrid
NO Ministerio de Economía y Competitividad (MINECO)
NO RETICS Program
DS Docta Complutense
RD 14 dic 2025