We report on in situ fluorescent quantification of the conjugation efficiency between azide-terminated synthetic polymers/ imaging probes and thiol-functionalized antibodies/proteins/peptides, by utilizing a doubly caged profluorescent and heterodifunctional core molecule (C1) as the self-sorting bridging unit. Orthogonal dual 'click' coupling of C1 with azide- and thiol-functionalized precursors leads to highly fluorescent bioconjugates, whereas single click products of C1 remain essentially nonfluorescent. This 'AND' logic gate-type fluorogenic feature also enables further integration with FRET processes. For the construction of antibody-probe conjugates from an anti-carcinoembryonic antigen and a quinone-caged profluorescent naphthalimide derivative, the dual 'click' coupling process with C1 can be conveniently monitored via emission turn-on of C1, whereas prominent changes in FRET ratios occur for antibody-probe conjugates when triggered by specific tumor-associated enzymes.
In Situ and Ex Situ Low-Field NMR Spectroscopy and MRI Endowed by SABRE Hyperpolarization
From The DNP-NMR Blog:
In Situ and Ex Situ Low-Field NMR Spectroscopy and MRI Endowed by SABRE Hyperpolarization
Barskiy, D.A., et al., In Situ and Ex Situ Low-Field NMR Spectroscopy and MRI Endowed by SABRE Hyperpolarization. ChemPhysChem, 2014. 15(18): p. 4100-7.
http://www.ncbi.nlm.nih.gov/pubmed/25367202
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12-15-2014 03:31 PM
[NMR paper] NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae.
NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae.
J Biol Chem. 2013 Oct 18;288(42):30597-606
Authors: Nedielkov R,...
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01-01-2014 03:05 PM
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
J Struct Biol. 2011 Apr 9;
Authors: Kodama Y, Reese ML, Shimba N, Ono K, Kanamori E, Dötsch V, Noguchi S, Fukunishi Y, Suzuki EI, Shimada I, Takahashi H
Protein-protein interactions are necessary for various cellular...
[NMR paper] In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-reson
In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-resonance NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-resonance NMR.
Arch Biochem Biophys. 1996 Sep 1;333(1):221-4
Authors: Klug CA, Burzio LA, Waite JH, Schaefer J
Rotational-echo double-resonance (REDOR) 13C NMR spectra with 2H dephasing have been obtained from plaques and threads from the byssus of...
Double-Caging Linker for AND-Type Fluorogenic Construction of Protein/Antibody Bioconjugates and in situ Quantification
Linear Mode
