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Biomimetic strategies for sensing biological species.

Hussain M, Wackerlig J, Lieberzeit PA - Biosensors (Basel) (2013)

Bottom Line: A different strategy comprises of devising polymer coatings to change the biocompatibility of surfaces that can also be used to immobilized natural receptors/ligands and thus stabilize them.Rationally speaking, this leads to self-assembled monolayers closely resembling cell membranes, sometimes also including bioreceptors.It mainly focuses on the literature published since 2005.

View Article: PubMed Central - PubMed

Affiliation: Department of Analytical Chemistry, University of Vienna, Waehringer Strasse 38, A-1090, Vienna, Austria; E-Mails: munawar_arif@hotmail.com (M.H.); judith.maehner@univie.ac.at (J.W.).

ABSTRACT
The starting point of modern biosensing was the application of actual biological species for recognition. Increasing understanding of the principles underlying such recognition (and biofunctionality in general), however, has triggered a dynamic field in chemistry and materials sciences that aims at joining the best of two worlds by combining concepts derived from nature with the processability of manmade materials, e.g., sensitivity and ruggedness. This review covers different biomimetic strategies leading to highly selective (bio)chemical sensors: the first section covers molecularly imprinted polymers (MIP) that attempt to generate a fully artificial, macromolecular mold of a species in order to detect it selectively. A different strategy comprises of devising polymer coatings to change the biocompatibility of surfaces that can also be used to immobilized natural receptors/ligands and thus stabilize them. Rationally speaking, this leads to self-assembled monolayers closely resembling cell membranes, sometimes also including bioreceptors. Finally, this review will highlight some approaches to generate artificial analogs of natural recognition materials and biomimetic approaches in nanotechnology. It mainly focuses on the literature published since 2005.

No MeSH data available.


Surface-imprinting strategies on pre-coated QCMs. (a) Aqueous monomer solution containing the template is dripped onto the transducer surface for self-organizing receptor sites on the thin film surface. (b) A stamp with densely packed trypsin crystals is pressed into the pre-polymerized coating, templates are removed after polymerization. Reprinted with permission from [10], © 2006 The Royal Society of Chemistry.
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biosensors-03-00089-f001: Surface-imprinting strategies on pre-coated QCMs. (a) Aqueous monomer solution containing the template is dripped onto the transducer surface for self-organizing receptor sites on the thin film surface. (b) A stamp with densely packed trypsin crystals is pressed into the pre-polymerized coating, templates are removed after polymerization. Reprinted with permission from [10], © 2006 The Royal Society of Chemistry.

Mentions: Firstly, let us regard “straightforward” protein imprinting: human immunodeficiency virus type 1 (HIV-1) related protein (glycoprotein 41, gp41), for instance, has attracted scientific interest, because it is the transmembrane protein of HIV-1 and plays a crucial role in membrane fusion between individual virions and T cells during infection. As such, it plays an important role in the efficacy of therapeutic intervention, because it indicates the extent of HIV-1 disease progression. By implementing the epitope imprinting strategy—where only a substructure of the analyte of interest is used as a template—Lu et al. [8] developed a biomimetic sensor to detect gp41. They used quartz crystal microbalance as a transducer and employed dopamine as the functional monomer. They polymerized it in the presence of a synthetic peptide consisting of 35 amino acids corresponding to position 579–613 of the gp41 sequence. It turned out, that the hydrophilic MIP shows substantial affinity towards the target analyte. The dissociation constant (Kd) of MIP for the template peptide was similar to that of monoclonal antibodies, namely 3.17 nM, calculated through Scatchard analysis. A limit of detection (LoD) of 2 ng/mL was achieved and practical performance was tested on real samples of human urine with satisfactory results. According to the authors, these LoD of HIV-1 gp41 were comparable to the reported ELISA method. On the basis of high its hydrophilicity and biocompatibility, dopamine excels over other functional monomers for this application. Furthermore, this simple epitope method can be adapted to other biomolecules. A further diagnostically important protein is myoglobin, which, among others, can be utilized as a cardiac marker. Rather than going for conventional epitope imprinting, Liao et al. [9] presented a surface imprinting strategy. For this purpose, they synthesized the Myo-MIP and established a mass spectrometry-based profiling system for assessing its selectivity compared to other proteins, such as histidine-rich glycoprotein, immunoglobulins, proapolipoprotein, and leech-derived tryptase inhibitor. Whereas the Myo-MIP indeed proved selective, the corresponding NIP (non-imprinted polymer) did not show any sensor signal. Generally speaking, surface imprinting is a versatile technique for protein imprinting: Hayden et al. [10], for instance, used 10 MHz QCM as transducers for MIP employing amorphous, crystalline and solubilized trypsin, respectively. The different strategies are summarized in Figure 1.


Biomimetic strategies for sensing biological species.

Hussain M, Wackerlig J, Lieberzeit PA - Biosensors (Basel) (2013)

Surface-imprinting strategies on pre-coated QCMs. (a) Aqueous monomer solution containing the template is dripped onto the transducer surface for self-organizing receptor sites on the thin film surface. (b) A stamp with densely packed trypsin crystals is pressed into the pre-polymerized coating, templates are removed after polymerization. Reprinted with permission from [10], © 2006 The Royal Society of Chemistry.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4263596&req=5

biosensors-03-00089-f001: Surface-imprinting strategies on pre-coated QCMs. (a) Aqueous monomer solution containing the template is dripped onto the transducer surface for self-organizing receptor sites on the thin film surface. (b) A stamp with densely packed trypsin crystals is pressed into the pre-polymerized coating, templates are removed after polymerization. Reprinted with permission from [10], © 2006 The Royal Society of Chemistry.
Mentions: Firstly, let us regard “straightforward” protein imprinting: human immunodeficiency virus type 1 (HIV-1) related protein (glycoprotein 41, gp41), for instance, has attracted scientific interest, because it is the transmembrane protein of HIV-1 and plays a crucial role in membrane fusion between individual virions and T cells during infection. As such, it plays an important role in the efficacy of therapeutic intervention, because it indicates the extent of HIV-1 disease progression. By implementing the epitope imprinting strategy—where only a substructure of the analyte of interest is used as a template—Lu et al. [8] developed a biomimetic sensor to detect gp41. They used quartz crystal microbalance as a transducer and employed dopamine as the functional monomer. They polymerized it in the presence of a synthetic peptide consisting of 35 amino acids corresponding to position 579–613 of the gp41 sequence. It turned out, that the hydrophilic MIP shows substantial affinity towards the target analyte. The dissociation constant (Kd) of MIP for the template peptide was similar to that of monoclonal antibodies, namely 3.17 nM, calculated through Scatchard analysis. A limit of detection (LoD) of 2 ng/mL was achieved and practical performance was tested on real samples of human urine with satisfactory results. According to the authors, these LoD of HIV-1 gp41 were comparable to the reported ELISA method. On the basis of high its hydrophilicity and biocompatibility, dopamine excels over other functional monomers for this application. Furthermore, this simple epitope method can be adapted to other biomolecules. A further diagnostically important protein is myoglobin, which, among others, can be utilized as a cardiac marker. Rather than going for conventional epitope imprinting, Liao et al. [9] presented a surface imprinting strategy. For this purpose, they synthesized the Myo-MIP and established a mass spectrometry-based profiling system for assessing its selectivity compared to other proteins, such as histidine-rich glycoprotein, immunoglobulins, proapolipoprotein, and leech-derived tryptase inhibitor. Whereas the Myo-MIP indeed proved selective, the corresponding NIP (non-imprinted polymer) did not show any sensor signal. Generally speaking, surface imprinting is a versatile technique for protein imprinting: Hayden et al. [10], for instance, used 10 MHz QCM as transducers for MIP employing amorphous, crystalline and solubilized trypsin, respectively. The different strategies are summarized in Figure 1.

Bottom Line: A different strategy comprises of devising polymer coatings to change the biocompatibility of surfaces that can also be used to immobilized natural receptors/ligands and thus stabilize them.Rationally speaking, this leads to self-assembled monolayers closely resembling cell membranes, sometimes also including bioreceptors.It mainly focuses on the literature published since 2005.

View Article: PubMed Central - PubMed

Affiliation: Department of Analytical Chemistry, University of Vienna, Waehringer Strasse 38, A-1090, Vienna, Austria; E-Mails: munawar_arif@hotmail.com (M.H.); judith.maehner@univie.ac.at (J.W.).

ABSTRACT
The starting point of modern biosensing was the application of actual biological species for recognition. Increasing understanding of the principles underlying such recognition (and biofunctionality in general), however, has triggered a dynamic field in chemistry and materials sciences that aims at joining the best of two worlds by combining concepts derived from nature with the processability of manmade materials, e.g., sensitivity and ruggedness. This review covers different biomimetic strategies leading to highly selective (bio)chemical sensors: the first section covers molecularly imprinted polymers (MIP) that attempt to generate a fully artificial, macromolecular mold of a species in order to detect it selectively. A different strategy comprises of devising polymer coatings to change the biocompatibility of surfaces that can also be used to immobilized natural receptors/ligands and thus stabilize them. Rationally speaking, this leads to self-assembled monolayers closely resembling cell membranes, sometimes also including bioreceptors. Finally, this review will highlight some approaches to generate artificial analogs of natural recognition materials and biomimetic approaches in nanotechnology. It mainly focuses on the literature published since 2005.

No MeSH data available.