Investigating the properties of TBA variants with twin thrombin binding domains(247 views) Amato T, Virgilio A, Pirone L, Vellecco V, Bucci M, Pedone E, Esposito V, Galeone A
Sci Rep (ISSN: 2045-2322linking, 2045-2322electronic), 2019 Jun 24; 9(1): 9184-9184.
Dipartimento di Farmacia, Universita degli Studi di Napoli Federico II, Via D. Montesano 49, 80131, Napoli, Italy., Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy., Dipartimento di Farmacia, Universita degli Studi di Napoli Federico II, Via D. Montesano 49, 80131, Napoli, Italy. verespos@unina.it., Dipartimento di Farmacia, Universita degli Studi di Napoli Federico II, Via D. Montesano 49, 80131, Napoli, Italy. galeone@unina.it.,
References: Not available.
Investigating the properties of TBA variants with twin thrombin binding domains
In this paper, we report studies concerning thrombin binding aptamer (TBA) dimeric derivatives in which the 3'-ends of two TBA sequences have been joined by means of linkers containing adenosine or thymidine residues and/or a glycerol moiety. CD and electrophoretic investigations indicate that all modified aptamers are able to form G-quadruplex domains resembling that of the parent TBA structure. However, isothermal titration calorimetry measurements of the aptamer/thrombin interaction point to different affinities to the target protein, depending on the type of linker. Consistently, the best ligands for thrombin show anticoagulant activities higher than TBA. Interestingly, two dimeric aptamers with the most promising properties also show far higher resistances in biological environment than TBA.
Investigating the properties of TBA variants with twin thrombin binding domains