A new assay design for clinical diagnostics based on alternative recognition elements

Albrecht, Christiane; Fechner, Peter; Honcharenko, Dmytro; Baltzer, Lars; Gauglitz, G.

doi:10.1016/j.bios.2010.03.022

Cited by 24 publications

(21 citation statements)

References 17 publications

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“…The values of (a) the binding rate coefficient, k and the fractal dimension, D f for a single-fractal analysis, (b) the binding rate coefficients, k 1 and k 2 and the fractal dimensions, D f1 and D f2 for a dual-fractal analysis, and (c) the dissociation rate coefficient, k d and the fractal dimension, D fd for a single-fractal analysis are given in Tables 11.4(a) and (b). Albrecht et al (2010) have recently presented a new assay design for clinical diagnostics based on alternative recognition. These indicate that the assay format has an important impact in the practical handling as well in the sensitivity of the testing results.…”

Section: Resultsmentioning

confidence: 99%

“…In this chapter we analyze the binding and dissociation kinetics (if applicable) of (1) IFN-gamma as a function of aptamer variants and inclusion of spacer in addition to spacer (Tuleuova et al, 2010), (2) GST-N protein in PBS and GST-N protein in 10-fold diluted serum to an LPSCF fiber-optic biosensor (Huang et al, 2009), (3) cytochrome c mutant to a superoxide biosensor (Wegerich et al, 2009), (4) CA-II to an ABS ligand on an SPR biosensor surface (Williams et al, 2009), (5) glycerol secretion from differentiated (murine 3T3-L1) adipocytes to a microfluidic platform for fluorescence-based assay (Clark et al, 2010), and (6) different concentrations of CRP in solution to a sandwich-type assay using a label-free detection method, reflectometric interference spectroscopy (Albrecht et al, 2010).…”

Section: Theorymentioning

confidence: 99%

See 1 more Smart Citation

Detection of Biomarkers for Different Diseases on Biosensor Surfaces Part II

Sadana

2015

Biomarkers and Biosensors

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Section: Resultsmentioning

confidence: 99%

Section: Theorymentioning

confidence: 99%

Detection of Biomarkers for Different Diseases on Biosensor Surfaces Part II

Sadana

2015

Biomarkers and Biosensors

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“…Very interesting applications can be developed when the coil also acts as an ion channel: in this way the binding activity is directly obtained within the signalgenerating molecule, and target detection can be performed by electrochemical approaches [54,55]. The coiled-coil peptide can also be chemically modified in order to add interacting groups, and a reflectometric interference sensor for C-reactive protein has been generated in this way [56]. Our research group has patented a library of coiled-coil receptors for the detection of small organic targets [57].…”

Section: Peptide Receptors For Ligand Sensingmentioning

confidence: 99%

Short peptides as biosensor transducers

2011

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This review deals with short peptides (up to 50 amino acids) as biomimetic active recognition elements in sensing systems. Peptide-based sensors have been developed in recent years according to different strategies. Synthetic peptides have been designed on the basis of known interactions between single or a few amino acids and targets, with attention being paid to the presence of peptide motifs known to allow intermolecular self-organization of the sensing peptides over the sensor surface. Sensitive and sophisticated sensors have been obtained in this way, but the use of designed peptides is limited by severe difficulties in their in silico design. Short peptides from random phage display have been selected in a random way from large, unfocussed, and often preexisting and commercially available phage display libraries, with no design elements. Such peptides often perform better than antibodies, but they are difficult to select when the target is a small molecule because of the need to immobilize it with considerable modifications of its structure. Artificial, miniaturized receptors have been obtained from the reduction of the known sequence of a natural receptor down to a synthesizable and yet stable one. Alternatively, binding sites have been created over a designed, stable peptide scaffold. Short peptides have also been used as active elements for the detection of their own natural receptors: pathogenic bacteria have been detected with antimicrobial and cell-penetrating peptides, but key challenges such as detection of bacteria in real samples, improved sensitivity, and improved selectivity have to be faced. Peptide substrates have been conjugated to fluorescent quantum dots to obtain disposable sensors for protease activity with high sensitivity. Ferrocene-peptide conjugates have been used for electrochemical sensing of protease activity.

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“…Two CRP binder molecules were covalently immobilized on glass chips and evaluated by RifS for the purpose of detecting CRP in human serum. The binder technology is an excellent alternative to antibodies in chip-based detection formats as it provides an opportunity to implement large ranges of detection because of to the wide range of affinities that is obtained in the screening procedure [49]. …”

Section: Applicationsmentioning

confidence: 99%

Crossing borders to bind proteins—a new concept in protein recognition based on the conjugation of small organic molecules or short peptides to polypeptides from a designed set

Baltzer

2011

Anal Bioanal Chem

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A new concept for protein recognition and binding is highlighted. The conjugation of small organic molecules or short peptides to polypeptides from a designed set provides binder molecules that bind proteins with high affinities, and with selectivities that are equal to those of antibodies. The small organic molecules or peptides need to bind the protein targets but only with modest affinities and selectivities, because conjugation to the polypeptides results in molecules with dramatically improved binder performance. The polypeptides are selected from a set of only sixteen sequences designed to bind, in principle, any protein. The small number of polypeptides used to prepare high-affinity binders contrasts sharply with the huge libraries used in binder technologies based on selection or immunization. Also, unlike antibodies and engineered proteins, the polypeptides have unordered three-dimensional structures and adapt to the proteins to which they bind. Binder molecules for the C-reactive protein, human carbonic anhydrase II, acetylcholine esterase, thymidine kinase 1, phosphorylated proteins, the D-dimer, and a number of antibodies are used as examples to demonstrate that affinities are achieved that are higher than those of the small molecules or peptides by as much as four orders of magnitude. Evaluation by pull-down experiments and ELISA-based tests in human serum show selectivities to be equal to those of antibodies. Small organic molecules and peptides are readily available from pools of endogenous ligands, enzyme substrates, inhibitors or products, from screened small molecule libraries, from phage display, and from mRNA display. The technology is an alternative to established binder concepts for applications in drug development, diagnostics, medical imaging, and protein separation.

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A new assay design for clinical diagnostics based on alternative recognition elements

Cited by 24 publications

References 17 publications

Detection of Biomarkers for Different Diseases on Biosensor Surfaces Part II

Detection of Biomarkers for Different Diseases on Biosensor Surfaces Part II

Short peptides as biosensor transducers

Crossing borders to bind proteins—a new concept in protein recognition based on the conjugation of small organic molecules or short peptides to polypeptides from a designed set

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