Abstract:
:RNA aptamers for tumor necrosis factor-alpha (TNFα), for which functionality was demonstrated in L929 cells, show only little affinity for the protein in vitro. Detailed investigation of the aptamer-protein interaction by surface plasmon resonance and quartz crystal microbalance analysis revealed that affinity is not the only crucial parameter for efficacy and functionality of those aptamers. Instead, the sensitive equilibrium of the monomeric and homotrimeric form of soluble TNFα decides on aptamer binding. Our results show that the field of application and the source of TNFα have to be carefully defined before selection of aptamer sequences.
journal_name
Appl Biochem Biotechnoljournal_title
Applied biochemistry and biotechnologyauthors
Nübel C,Appel B,Hospach I,Mai M,Krasteva N,Nelles G,Petruschka L,Müller Sdoi
10.1007/s12010-016-2002-2subject
Has Abstractpub_date
2016-06-01 00:00:00pages
398-414issue
3eissn
0273-2289issn
1559-0291pii
10.1007/s12010-016-2002-2journal_volume
179pub_type
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