2007
DOI: 10.1080/15599610701672652
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Molecular Printing Using UV-Assisted Immobilization of Biomolecules

Abstract: UV light-assisted immobilization of biomolecules is a novel technology that is well suited for achieving spatially-localized covalent coupling of biomolecules onto thiol reactive surfaces, e.g., thiolated glass, silicon, or gold. The spatial resolution is defined by the area illuminated by the UV source. Thus, in principle, the limit will be the diffraction limit of the light. This enables printing of molecular arrays or other patterns onto a substrate with higher resolution and considerably faster than can be… Show more

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Cited by 6 publications
(5 citation statements)
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References 11 publications
(13 reference statements)
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“…Reduction of SS upon UV excitation of aromatic residues has been shown for proteins such as cutinase and lysozyme (Neves- Petersen et al, & 2002, bovine serum albumin (Skovsen et al, 2009a;Parracino et al, 2011) prostate specific antigen (Parracino et al, 2010), and antibody Fab fragments . As mentioned in the introduction, this phenomenon has led to a new technology for protein immobilization (LAMI, light assisted molecular immobilization) since the created thiol groups can bind thiol reactive surfaces leading to oriented covalent protein immobilization (Neves- Snabe et al, 2006;Duroux et al, 2007aDuroux et al, , 2007bDuroux et al, & 2007cSkovsen et al, 2007Skovsen et al, , 2009aSkovsen et al, & 2009bNeves-Petersen et al, 2009b;Parracino et al, 2010Parracino et al, & 2011.…”
Section: Tyrosinementioning
confidence: 99%
See 1 more Smart Citation
“…Reduction of SS upon UV excitation of aromatic residues has been shown for proteins such as cutinase and lysozyme (Neves- Petersen et al, & 2002, bovine serum albumin (Skovsen et al, 2009a;Parracino et al, 2011) prostate specific antigen (Parracino et al, 2010), and antibody Fab fragments . As mentioned in the introduction, this phenomenon has led to a new technology for protein immobilization (LAMI, light assisted molecular immobilization) since the created thiol groups can bind thiol reactive surfaces leading to oriented covalent protein immobilization (Neves- Snabe et al, 2006;Duroux et al, 2007aDuroux et al, , 2007bDuroux et al, & 2007cSkovsen et al, 2007Skovsen et al, , 2009aSkovsen et al, & 2009bNeves-Petersen et al, 2009b;Parracino et al, 2010Parracino et al, & 2011.…”
Section: Tyrosinementioning
confidence: 99%
“…5). The new protein immobilization technology has led to the development of (Neves- Snabe et al, 2006;Duroux et al, 2007aDuroux et al, , 2007bDuroux et al, & 2007cSkovsen et al, 2007Skovsen et al, , 2009aSkovsen et al, & 2009bNeves-Petersen et al, 2009b;Parracino et al, 2010Parracino et al, & 2011:…”
Section: Photochemistry Biosensor Microarrays and Drug Delivery Systemsmentioning
confidence: 99%
“…Reduction of SS upon UV excitation of aromatic residues has been shown for proteins such as cutinase and lysozyme (Neves- Petersen et al, & 2002, bovine serum albumin Parracino et al, 2011) prostate specific antigen , and antibody Fab fragments . As mentioned in the introduction, this phenomenon has led to a new technology for protein immobilization (LAMI, light assisted molecular immobilization) since the created thiol groups can bind thiol reactive surfaces leading to oriented covalent protein immobilization Snabe et al, 2006;Duroux et al, 2007aDuroux et al, , 2007bDuroux et al, & 2007cSkovsen et al, 2007Skovsen et al, , 2009aSkovsen et al, & 2009bNeves-Petersen et al, 2009b;Parracino et al, 2010Parracino et al, & 2011. Fig.…”
Section: Important Photochemical Mechanism In Disulphide Bridge Contamentioning
confidence: 99%
“…5). The new protein immobilization technology has led to the development of (Neves- Snabe et al, 2006;Duroux et al, 2007aDuroux et al, , 2007bDuroux et al, & 2007cSkovsen et al, 2007Skovsen et al, , 2009aSkovsen et al, & 2009bNevesPetersen et al, 2009b;Parracino et al, 2010Parracino et al, & 2011:…”
Section: Photochemistry Biosensor Microarrays and Drug Delivery Systemsmentioning
confidence: 99%
“…In addition, our method for producing photo-synthesis nanoparticles has many potential applications in molecular interactions and mapping of biotechnology. The photo-reduction of disulfide bonds buried in proteins provides a novel method to investigate not only protein folding/unfolding and intermolecular self-assembly, but also the immobilization, molecular printing and drug delivery system [27][28][29]. Based on these studies, the photo-synthesis of protein nanoparticles is showing more and more potential applications in the future.…”
Section: Introductionmentioning
confidence: 99%