| 1. |
|
|
| 2. |
- Choulier, Laurence, et al.
(författare)
-
Delineation of a linear epitope by multiple peptide synthesis and phage display
- 2001
-
Ingår i: JOURNAL OF IMMUNOLOGICAL METHODS. - : ELSEVIER SCIENCE BV. - 0022-1759. ; 249:1-2, s. 253-264
-
Tidskriftsartikel (refereegranskat)abstract
- Two different approaches, the phage display technique and the Spot peptide synthesis on cellulose membranes, were used to identify sequences recognized by Fab 57P specific for tobacco mosaic virus protein (TMVP), and define the preferred chemical composit
|
|
| 3. |
- Choulier, Laurence, et al.
(författare)
-
Environmentally Sensitive Fluorescent Sensors Based on Synthetic Peptides
- 2010
-
Ingår i: SENSORS. - : Molecular Diversity Preservation International (MDPI). - 1424-8220. ; 10:4, s. 3126-3144
-
Forskningsöversikt (refereegranskat)abstract
- Biosensors allow the direct detection of molecular analytes, by associating a biological receptor with a transducer able to convert the analyte-receptor recognition event into a measurable signal. We review recent work aimed at developing synthetic fluorescent molecular sensors for a variety of analytes, based on peptidic receptors labeled with environmentally sensitive fluorophores. Fluorescent indicators based on synthetic peptides are highly interesting alternatives to protein-based sensors, since they can be synthesized chemically, are stable, and can be easily modified in a site-specific manner for fluorophore coupling and for immobilization on solid supports.
|
|
| 4. |
- Enander, Karin, 1972-, et al.
(författare)
-
A peptide-based, ratiometric biosensor construct for direct fluorescence detection of a protein analyte
- 2008
-
Ingår i: Bioconjugate chemistry. - : American Chemical Society (ACS). - 1043-1802 .- 1520-4812. ; 19:9, s. 1864-1870
-
Tidskriftsartikel (refereegranskat)abstract
- We present the design, synthesis, and functional evaluation of peptide-based fluorescent constructs for wavelength-ratiometric biosensing of a protein analyte. The concept was shown using the high-affinity model interaction between the 18 amino acid peptide pTMVP and a recombinant antibody fragment, Fab57P. pTMVP was functionalized in two different positions with 6-bromomethyl-2-(2-furanyl)-3-hydroxychromone, an environmentally sensitive fluorophore with a two-band emission. The equilibrium dissociation constant of the interaction between pTMVP and Fab57P was largely preserved upon labeling. The biosensor ability of the labeled peptide constructs was evaluated in terms of the relative intensity change of the emission bands from the normal (N*) and tautomer (T*) excited-state species of the fluorophore (IN*/IT*) upon binding of Fab57P. When the peptide was labeled in the C terminus, the IN*/I T* ratio changed by 40% upon analyte binding, while labeling close to the residues most important for binding resulted in a construct that completely lacked ratiometric biosensor ability. Integrated biosensor elements for reagentless detection, where peptides and ratiometric fluorophores are combined to ensure robustness in both recognition and signaling, are expected to become an important contribution to the design of future protein quantification assays in immobilized formats. © 2008 American Chemical Society.
|
|
