112510-75-5Relevant articles and documents
Bathophenanthroline-ruthenium(II) complexes as non-radioactive labels for oligonucleotides which can be measured by time-resolved fluorescence techniques
Bannwarth,Schmidt,Stallard,Hornung,Knorr,Muller
, p. 2085 - 2099 (1988)
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5′-Tethered Stilbene Derivatives as Fidelity- and Affinity-Enhancing Modulators of DNA Duplex Stability
Dogan, Zeynep,Paulini, Ralph,Stuetz, Jan A. Rojas,Narayanan, Sukunath,Richert, Clemens
, p. 4762 - 4763 (2007/10/03)
A series of 5′-linked stilbene-DNA conjugates with different substituents in the distal aromatic ring of the stilbene was prepared, and the effect of the modifications on duplex stability was determined via UV-melting curves. A trimethoxystilbene derivative as a 5′-substituent increases duplex melting points by up to 12.2 °C per modification. With this alkoxystilbene substituent, terminal mismatches in DNA duplexes lower the melting point by up to 23.4 °C over the perfectly matched control, whereas terminal mismatches in unmodified DNA cause melting point depressions of no more than 6.1 °C. An aminomethylstilbene substituent linked to an oligopyrrolamide minor groove binder increases the melting point of an all-A/T decamer by up to 32.7 °C, thus shifting the melting point into a range typical for duplexes with statistical G/C-content. An affinity- and selectivity-enhancing effect was also observed when the trimethoxystilbene cap was employed on a small DNA microarray. The phosphoramidite of the trimethoxystilbene can be readily employed in automatic DNA synthesis, facilitating the generation of DNA chips with improved fidelity. Copyright
Fluoresceinated FKBP12 ligands for a high-throughput fluorescence polarization assay
Dubowchik, Gene M.,Ditta, Jonathan L.,Herbst, John J.,Bollini, Sagarika,Vinitsky, Alexander
, p. 559 - 562 (2007/10/03)
Several fluoresceinated FKBP12 ligands have been prepared for a high-throughput fluorescence polarization assay. K(i)s for FKBP12 rotamase inhibition by these ligands range from 1.3 μM to 32 nM, and their design is based on X-ray crystal structures of FKBP12 complexed with known immunophilin ligands. (C) 2000 Elsevier Science Ltd. All rights reserved.
