Immobilisation of proteins by atomic clusters on surfaces.
In this Opinion article, we describe a nanotechnology-based approach to immobilize and orient proteins onto surfaces using atomic clusters prepared by physical methods. This is relevant to future protein biochips where dilute arrays of protein binding sites, each designed to immobilize no more than one protein molecule, would be ideal. In the case of a surface consisting of size-selected atomic gold clusters, proteins containing free cysteine residues can chemisorb directly to the bare cluster surface, thus effecting oriented immobilisation. The selection of atomic gold clusters in the size range 1-100 atoms (<3nm in diameter) is intended to ensure that, typically, only one protein can bind directly to the cluster surface. These nanoclusters of a smaller size scale than that of the protein present minimal contact between the gold and the protein, and hence imply a reduced risk of protein denaturing compared with gold films or extended surfaces.
Palmer
Richard E
RE
Nanoscale Physics Research Laboratory, School of Physics and Astronomy, The University of Birmingham, Edgbaston, Birmingham B15 2TT, UK. r.e.palmer@bham.ac.uk
Leung
Carl
C
D001665:Binding Sites / Q000502:physiology*; D003545:Cysteine / Q000737:chemistry; D006046:Gold / Q000737:chemistry*; D049452:Green Fluorescent Proteins / Q000737:chemistry; D006735:Horseradish Peroxidase / Q000737:chemistry; D018625:Microscopy, Atomic Force; D036103:Nanotechnology / Q000379:methods*; D053683:Oncostatin M / Q000737:chemistry; D040081:Protein Array Analysis / Q000379:methods*; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification
C508351:OSM protein, human; D011506:Proteins; D053683:Oncostatin M; D049452:Green Fluorescent Proteins; D006046:Gold; D006735:Horseradish Peroxidase; D003545:Cysteine