10 Aptamers for Thrombotic Diseases
313
39. Schwienhorst A (2006) Direct thrombin inhibitors—a survey of recent developments. Cell
Mol Life Sci 63(23):2773–2791
40. Kretz CA, Stafford AR, Fredenburgh JC, Weitz JI (2006) HD1, a thrombin-directed aptamer,
binds exosite 1 on prothrombin with high affinity and inhibits its activation by prothrombinase.
J Biol Chem 281(49):37477–37485
41. Muller J, Freitag D, Mayer G, Potzsch B (2008) Anticoagulant characteristics of HD1-22, a
bivalent aptamer that specifically inhibits thrombin and prothrombinase. J Thromb Haemost
6(12):2105–2112
42. Mayer G, Rohrbach F, Potzsch B, Muller J (2011) Aptamer-based modulation of blood
coagulation. Hamostaseologie 31(4):258–263
43. Hughes QW, Le BT, Gilmore G, Baker RI, Veedu RN (2017) Construction of a Bivalent Thrombin Binding Aptamer and Its Antidote with Improved Properties. Molecules
22(10):1170
44. Gomez-Outes A, Suarez-Gea ML, Lecumberri R, Rocha E, Pozo-Hernandez C, VargasCastrillon E (2011) New parenteral anticoagulants in development. Ther Adv Cardiovasc
Dis 5(1):33–59
45. Stoll H, Steinle H, Wilhelm N, Hann L, Kunnakattu SJ, Narita M, Schlensak C, Wendel
HP, Avci-Adali M (2017) Rapid Complexation of Aptamers by Their Specific Antidotes.
Molecules 22(6):954
46. Troisi R, Napolitano V, Spiridonova V, Russo KI, Sica F (2018) Several structural motifs cooperate in determining the highly effective anti-thrombin activity of NU172 aptamer. Nucleic
Acids Res 46(22):12177–12185
47. Kunnakattu SJ, Hann L, Kurz J, Haag H, Fennrich S, Rauch N, Schlensak C, Wendel
HP, Stoppelkamp S, Avci-Adali M (2019) Application of Piezo-Based Measuring System
for Evaluation of Nucleic Acid-Based Drugs Influencing the Coagulation. Sensors (Basel)
20(1):152
48. Bompiani KM, Monroe DM, Church FC, Sullenger BA (2012) A high affinity, antidotecontrollable prothrombin and thrombin-binding RNA aptamer inhibits thrombin generation
and thrombin activity. J Thromb Haemost 10(5):870–880
49. Long SB, Long MB, White RR, Sullenger BA (2008) Crystal structure of an RNA aptamer
bound to thrombin. RNA 14(12):2504–2512
50. White R, Rusconi C, Scardino E, Wolberg A, Lawson J, Hoffman M, Sullenger B (2001)
Generation of species cross-reactive aptamers using “toggle” SELEX. Mol Ther 4(6):567–573
51. Zavyalova E, Golovin A, Pavlova G, Kopylov A (2013) Module-activity relationship of Gquadruplex based DNA aptamers for human thrombin. Curr Med Chem 20(38):4836–4843
52. Zavyalova E, Samoylenkova N, Revishchin A, Turashev A, Gordeychuk I, Golovin A, Kopylov
A, PavlovaG (2017) The Evaluation of Pharmacodynamics and Pharmacokinetics of Antithrombin DNA Aptamer RA-36. Front Pharmacol 8:922
53. Zavyalova E, Samoylenkova N, Revishchin A, Golovin A, Pavlova G, Kopylov A (2014)
Evaluation of antithrombotic activity of thrombin DNA aptamers by a murine thrombosis
model. PLoS ONE 9(9):e107113
54. Mazurov AV, Titaeva EV, Khaspekova SG, Storojilova AN, Spiridonova VA, Kopylov AM,
Dobrovolsky AB (2011) Characteristics of a new DNA aptamer, direct inhibitor of thrombin.
Bull Exp Biol Med 150(4):422–425
55. Russo KI, Spiridonova V, Pica A, Napolitano V, Sica F (2016) Different duplex/quadruplex
junctions determine the properties of anti-thrombin aptamers with mixed folding. Nucleic
Acids Res 44(2):983–991
56. Spiridonova VA, Novikova TM, Nikulina DM, Shishkina TA, Golubkina EV, Dyukareva OS,
Trizno NN (2018) Complex formation with protamine prolongs the thrombin-inhibiting effect
of DNA aptamer in vivo. Biochimie 145:158–162
57. Kotkowiak W, Wengel J, Scotton CJ, Pasternak A (2019) Improved RE31 Analogues
Containing Modified Nucleic Acid Monomers: Thermodynamic, Structural, and Biological
Effects. J Med Chem 62(5):2499–2507
313
39. Schwienhorst A (2006) Direct thrombin inhibitors—a survey of recent developments. Cell
Mol Life Sci 63(23):2773–2791
40. Kretz CA, Stafford AR, Fredenburgh JC, Weitz JI (2006) HD1, a thrombin-directed aptamer,
binds exosite 1 on prothrombin with high affinity and inhibits its activation by prothrombinase.
J Biol Chem 281(49):37477–37485
41. Muller J, Freitag D, Mayer G, Potzsch B (2008) Anticoagulant characteristics of HD1-22, a
bivalent aptamer that specifically inhibits thrombin and prothrombinase. J Thromb Haemost
6(12):2105–2112
42. Mayer G, Rohrbach F, Potzsch B, Muller J (2011) Aptamer-based modulation of blood
coagulation. Hamostaseologie 31(4):258–263
43. Hughes QW, Le BT, Gilmore G, Baker RI, Veedu RN (2017) Construction of a Bivalent Thrombin Binding Aptamer and Its Antidote with Improved Properties. Molecules
22(10):1170
44. Gomez-Outes A, Suarez-Gea ML, Lecumberri R, Rocha E, Pozo-Hernandez C, VargasCastrillon E (2011) New parenteral anticoagulants in development. Ther Adv Cardiovasc
Dis 5(1):33–59
45. Stoll H, Steinle H, Wilhelm N, Hann L, Kunnakattu SJ, Narita M, Schlensak C, Wendel
HP, Avci-Adali M (2017) Rapid Complexation of Aptamers by Their Specific Antidotes.
Molecules 22(6):954
46. Troisi R, Napolitano V, Spiridonova V, Russo KI, Sica F (2018) Several structural motifs cooperate in determining the highly effective anti-thrombin activity of NU172 aptamer. Nucleic
Acids Res 46(22):12177–12185
47. Kunnakattu SJ, Hann L, Kurz J, Haag H, Fennrich S, Rauch N, Schlensak C, Wendel
HP, Stoppelkamp S, Avci-Adali M (2019) Application of Piezo-Based Measuring System
for Evaluation of Nucleic Acid-Based Drugs Influencing the Coagulation. Sensors (Basel)
20(1):152
48. Bompiani KM, Monroe DM, Church FC, Sullenger BA (2012) A high affinity, antidotecontrollable prothrombin and thrombin-binding RNA aptamer inhibits thrombin generation
and thrombin activity. J Thromb Haemost 10(5):870–880
49. Long SB, Long MB, White RR, Sullenger BA (2008) Crystal structure of an RNA aptamer
bound to thrombin. RNA 14(12):2504–2512
50. White R, Rusconi C, Scardino E, Wolberg A, Lawson J, Hoffman M, Sullenger B (2001)
Generation of species cross-reactive aptamers using “toggle” SELEX. Mol Ther 4(6):567–573
51. Zavyalova E, Golovin A, Pavlova G, Kopylov A (2013) Module-activity relationship of Gquadruplex based DNA aptamers for human thrombin. Curr Med Chem 20(38):4836–4843
52. Zavyalova E, Samoylenkova N, Revishchin A, Turashev A, Gordeychuk I, Golovin A, Kopylov
A, PavlovaG (2017) The Evaluation of Pharmacodynamics and Pharmacokinetics of Antithrombin DNA Aptamer RA-36. Front Pharmacol 8:922
53. Zavyalova E, Samoylenkova N, Revishchin A, Golovin A, Pavlova G, Kopylov A (2014)
Evaluation of antithrombotic activity of thrombin DNA aptamers by a murine thrombosis
model. PLoS ONE 9(9):e107113
54. Mazurov AV, Titaeva EV, Khaspekova SG, Storojilova AN, Spiridonova VA, Kopylov AM,
Dobrovolsky AB (2011) Characteristics of a new DNA aptamer, direct inhibitor of thrombin.
Bull Exp Biol Med 150(4):422–425
55. Russo KI, Spiridonova V, Pica A, Napolitano V, Sica F (2016) Different duplex/quadruplex
junctions determine the properties of anti-thrombin aptamers with mixed folding. Nucleic
Acids Res 44(2):983–991
56. Spiridonova VA, Novikova TM, Nikulina DM, Shishkina TA, Golubkina EV, Dyukareva OS,
Trizno NN (2018) Complex formation with protamine prolongs the thrombin-inhibiting effect
of DNA aptamer in vivo. Biochimie 145:158–162
57. Kotkowiak W, Wengel J, Scotton CJ, Pasternak A (2019) Improved RE31 Analogues
Containing Modified Nucleic Acid Monomers: Thermodynamic, Structural, and Biological
Effects. J Med Chem 62(5):2499–2507