Novel photonic technique creates micrometer resolution protein arrays and provides a new approach to coupling of genes, peptide hormones and drugs to nanoparticle carriers

被引:12
作者
Duroux, M. [1 ]
Duroux, L. [1 ]
Neves-Petersen, M. T. [1 ]
Skovsen, E. [1 ]
Petersen, S. B. [1 ]
机构
[1] Aalborg Univ, Dept Phys & Nanotechnol, DK-9220 Aalborg, Denmark
关键词
light-assisted protein immobilization; UV light; disulphide bridges; micro-arrays; micro-dispensing; nanoparticles; IMMOBILIZATION;
D O I
10.1016/j.apsusc.2007.02.131
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
We demonstrate that ultraviolet light can be used to make sterically oriented covalent immobilization of a large variety of protein molecules onto either thiolated quartz, gold or silicon. The reaction mechanism behind the reported new technology involves light-induced breakage of disulphide bridges in proteins upon UV illumination of nearby aromatic amino acids, resulting in the formation of free, reactive thiol groups that will form covalent bonds with thiol reactive surfaces. In general, the protein molecules retain their function. The size of the immobilization spot is limited to the focal point of illumination being as small as a few micrometers. This new technology allows for dense packing of different biomolecules on a surface, allowing the creation of multi-potent functionalised new materials, such as nano-biosensors. We have developed the necessary technology for preparing large protein arrays of enzymes and fragments of monoclonal antibodies. Dedicated image processing software has been developed for making quality assessment of the protein arrays. This novel technology is ideal to couple drugs and other bio-molecules to nanoparticles which can be used as carriers into cells for therapeutic purposes. (c) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码:8125 / 8129
页数:5
相关论文
共 15 条
[1]   ORIENTED AND COVALENT IMMOBILIZATION OF TARGET MOLECULES TO SOLID SUPPORTS - SYNTHESIS AND APPLICATION OF A LIGHT-ACTIVATABLE AND THIOL-REACTIVE CROSS-LINKING REAGENT [J].
COLLIOUD, A ;
CLEMENCE, JF ;
SANGER, M ;
SIGRIST, H .
BIOCONJUGATE CHEMISTRY, 1993, 4 (06) :528-536
[2]   The convergence of synthetic organic and polymer chemistries [J].
Hawker, CJ ;
Wooley, KL .
SCIENCE, 2005, 309 (5738) :1200-1205
[3]   Conservation of cys-cys trp structural triads and their geometry in the protein domains of immunoglobulin superfamily members [J].
Ioerger, TR ;
Du, CG ;
Linthicum, DS .
MOLECULAR IMMUNOLOGY, 1999, 36 (06) :373-386
[4]   IMMOBILIZATION OF PROTEINS TO A CARBOXYMETHYLDEXTRAN-MODIFIED GOLD SURFACE FOR BIOSPECIFIC INTERACTION ANALYSIS IN SURFACE-PLASMON RESONANCE SENSORS [J].
JOHNSSON, B ;
LOFAS, S ;
LINDQUIST, G .
ANALYTICAL BIOCHEMISTRY, 1991, 198 (02) :268-277
[5]   Nanomedicine: current status and future prospects [J].
Moghimi, SM ;
Hunter, AC ;
Murray, JC .
FASEB JOURNAL, 2005, 19 (03) :311-330
[6]   Photonic activation of disulfide bridges achieves oriented protein immobilization on biosensor surfaces [J].
Neves-Petersen, MT ;
Snabe, T ;
Klitgaard, S ;
Duroux, M ;
Petersen, SB .
PROTEIN SCIENCE, 2006, 15 (02) :343-351
[7]   High probability of disrupting a disulphide bridge mediated by an endogenous excited tryptophan residue [J].
Neves-Petersen, MT ;
Gryczynski, Z ;
Lakowicz, J ;
Fojan, P ;
Pedersen, S ;
Petersen, E ;
Petersen, SB .
PROTEIN SCIENCE, 2002, 11 (03) :588-600
[8]  
NEVESPETERSEN MT, 2005, Patent No. 200500956
[9]  
NEVESPETERSEN MT, 2004, Patent No. 2004065928
[10]   Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase [J].
Prompers, JJ ;
Hilbers, CW ;
Pepermans, HAM .
FEBS LETTERS, 1999, 456 (03) :409-416