Plasmonics for the study of metal ion-protein interactions.
The study of metal-protein interactions is an expanding field of research investigated by bioinorganic chemists as it has wide applications in biological systems. Very recently, it has been reported that it is possible to study metal-protein interactions by immobilizing biomolecules on metal surfaces and applying experimental approaches based on plasmonics which have usually been used to investigate protein-protein interactions. This is possible because the electronic structure of metals generates plasmons whose properties can be exploited to obtain information from biomolecules that interact not only with other molecules but also with ions in solution. One major challenge of such approaches is to immobilize the protein to be studied on a metal surface with preserved native structure. This review reports and discusses all the works that deal with such an expanding new field of application of plasmonics with specific attention to surface plasmon resonance, highlighting the advantages and drawbacks of such approaches in comparison with other experimental techniques traditionally used to study metal-protein interactions.
Dipartimento di Scienze Chimiche, Università di Catania, Viale Andrea Doria 6, 95125 Catania, Italy. grassog@unict.it
Giuseppe
G
Grasso
Giuseppe
G
Spoto
D002413:Cations, Divalent; D002414:Cations, Monovalent; D006801:Humans; D008670:Metals / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D057165:Proteostasis Deficiencies / Q000378:metabolism* / Q000473:pathology; D021241:Spectrometry, Mass, Electrospray Ionization; D017550:Spectroscopy, Fourier Transform Infrared; D020349:Surface Plasmon Resonance / Q000379:methods*
D002413:Cations, Divalent; D002414:Cations, Monovalent; D008670:Metals; D011506:Proteins