Oriented coupling of major histocompatibility complex (MHC) to sensor surfaces using light assisted immobilisation technology
Research output: Contribution to journal › Journal article › Research › peer-review
Controlled and oriented immobilisation of proteins for biosensor purposes is of extreme interest since this provides more efficient sensors with a larger density of active binding sites per area compared to sensors produced by conventional immobilisation. In this paper oriented coupling of a major histocompatibility complex (MHC class I) to a sensor surface is presented. The coupling was performed using light assisted immobilisation--a novel immobilisation technology which allows specific opening of particular disulphide bridges in proteins which then is used for covalent bonding to thiol-derivatised surfaces via a new disulphide bond. Light assisted immobilisation specifically targets the disulphide bridge in the MHC-I molecule alpha(3)-domain which ensures oriented linking of the complex with the peptide binding site exposed away from the sensor surface. Structural analysis reveals that a similar procedure can be used for covalent immobilisation of MHC class II complexes. The results open for the development of efficient T cell sensors, sensors for recognition of peptides of pathogenic origin, as well as other applications that may benefit from oriented immobilisation of MHC proteins.
Original language | English |
---|---|
Journal | Biosensors and Bioelectronics |
Volume | 21 |
Issue number | 8 |
Pages (from-to) | 1553-9 |
Number of pages | 6 |
ISSN | 0956-5663 |
DOIs | |
Publication status | Published - 2005 |
Bibliographical note
Keywords: Adsorption; Biosensing Techniques; Biotechnology; Coated Materials, Biocompatible; Crystallization; Histocompatibility Antigens Class I; Protein Array Analysis; Protein Binding; Ultraviolet Rays
ID: 9942912