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Your search keyword '"Baud-Demattei, M. V."' showing total 5 results
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5 results on '"Baud-Demattei, M. V."'

1. Alpha-beta chimeric oligonucleotides form a new stable 'snail-like' structure

Author

Gottikh, M.B., Fedorova, O.A., Baud-Demattei, M.-V., Giorgi-Renault, S., Bertrand, J.-R., Shabarova, Z.A., and Malvy, C.

Subjects
Nucleotides -- Research, Molecular probes -- Research, Nucleic acid probes -- Research, Chemistry
Abstract

A chimeric alpha-beta-oligonucleotide (ODN) with a 3'-end alpha-sequence complementary to its 5'-end beta-sequence is described as an alternative to the search for new ODN structures that exhibited greater resistance to nucleases than natural oligodeoxyribonucleotides. The 3'-end alpha-sequence of the chimeric alpha-beta-ODN formed a stable parallel duplex with its 5'-end beta-sequence. The molecule showed high resistance to nuclease attack due to its inner duplex formation.

Published
1996

5. In vitro inhibition of the pim-1 protooncogene by chimeric oligodeoxyribonucleotides composed of alpha- and beta-anomeric fragments.

Author

Gottikh M, Baud-Demattei MV, Lescot E, Giorgi-Renault S, Shabarova Z, Dautry F, Malvy C, and Bertrand JR

Subjects
Animals, Base Sequence, Blood, Culture Media, Erythroblasts, Globins genetics, Humans, Hydrolysis, Mice, Molecular Sequence Data, Oligonucleotides, Antisense metabolism, Protein Biosynthesis, Proto-Oncogene Proteins antagonists & inhibitors, Proto-Oncogene Proteins c-pim-1, RNA, Messenger genetics, RNA, Messenger metabolism, Rabbits, Ribonuclease H metabolism, Oligonucleotides, Antisense pharmacology, Protein Serine-Threonine Kinases, Proto-Oncogene Proteins genetics
Abstract

We show that oligodeoxyribonucleotides (oligos) composed of alpha- and beta-anomeric sections can be used as antisense compounds. An octamer has been chosen as an effector domain to form a substrate for RNaseH. This octamer is complementary to the translation start site of the pim-1 protooncogene mRNA. Chimeric alpha-beta oligos and their beta-analogs have a similar binding affinity for their target. These oligos also direct efficient RNaseH-mediated cleavage of target mRNA. Among all alpha-beta oligos studied, one with an alpha-fragment bound by its 3'-end to the 3'-end of the beta-octamer is the most resistant to nucleolytic digestion in biological media. The alpha-beta oligos have been found to inhibit in vitro translation of pim-1 RNA with specificity.

Published
1994
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