TY  - JOUR
AU  - Opsenica, Igor
AU  - Filipović, Vuk
AU  - Nuss, Jon E.
AU  - Gomba, Laura M.
AU  - Opsenica, Dejan M.
AU  - Burnett, James C.
AU  - Gussio, Rick
AU  - Šolaja, Bogdan A.
AU  - Bavari, Sina
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1314
AB  - Botulinum neurotoxins (BoNTs), composed of a family of seven serotypes (categorized A-G), are the deadliest of known biological toxins. The activity of the metalloprotease, light chain (LC) component of the toxins is responsible for causing the life-threatening paralysis associated with the disease botulism. Herein we report significantly more potent analogs of novel, lead BoNT serotype A LC inhibitor 2,5-bis(4-amidinophenyl)thiophene (K-i = 10.881 mu M +/- 0.90 mu M). Specifically, synthetic modifications involved simultaneously replacing the lead inhibitor's terminal bis-amidines with secondary amines and the systematic tethering of 4-amino-7-chloroquinoline substituents to provide derivatives with K-i values ranging from 0.302 mu M (+/- 0.03 mu M) to 0.889 mu M (+/- 0.11 mu M). (C) 2012 Elsevier Masson SAS. All rights reserved.
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Paris
T2  - European Journal of Medicinal Chemistry
T1  - The synthesis of 2,5-bis(4-amidinophenyl)thiophene derivatives providing submicromolar-range inhibition of the botulinum neurotoxin serotype A metalloprotease
VL  - 53
SP  - 374
EP  - 379
DO  - 10.1016/j.ejmech.2012.03.043
ER  - 

@article{
author = "Opsenica, Igor and Filipović, Vuk and Nuss, Jon E. and Gomba, Laura M. and Opsenica, Dejan M. and Burnett, James C. and Gussio, Rick and Šolaja, Bogdan A. and Bavari, Sina",
year = "2012",
abstract = "Botulinum neurotoxins (BoNTs), composed of a family of seven serotypes (categorized A-G), are the deadliest of known biological toxins. The activity of the metalloprotease, light chain (LC) component of the toxins is responsible for causing the life-threatening paralysis associated with the disease botulism. Herein we report significantly more potent analogs of novel, lead BoNT serotype A LC inhibitor 2,5-bis(4-amidinophenyl)thiophene (K-i = 10.881 mu M +/- 0.90 mu M). Specifically, synthetic modifications involved simultaneously replacing the lead inhibitor's terminal bis-amidines with secondary amines and the systematic tethering of 4-amino-7-chloroquinoline substituents to provide derivatives with K-i values ranging from 0.302 mu M (+/- 0.03 mu M) to 0.889 mu M (+/- 0.11 mu M). (C) 2012 Elsevier Masson SAS. All rights reserved.",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Paris",
journal = "European Journal of Medicinal Chemistry",
title = "The synthesis of 2,5-bis(4-amidinophenyl)thiophene derivatives providing submicromolar-range inhibition of the botulinum neurotoxin serotype A metalloprotease",
volume = "53",
pages = "374-379",
doi = "10.1016/j.ejmech.2012.03.043"
}

Opsenica, I., Filipović, V., Nuss, J. E., Gomba, L. M., Opsenica, D. M., Burnett, J. C., Gussio, R., Šolaja, B. A.,& Bavari, S.. (2012). The synthesis of 2,5-bis(4-amidinophenyl)thiophene derivatives providing submicromolar-range inhibition of the botulinum neurotoxin serotype A metalloprotease. in European Journal of Medicinal Chemistry
Elsevier France-Editions Scientifiques Medicales Elsevier, Paris., 53, 374-379.
https://doi.org/10.1016/j.ejmech.2012.03.043

Opsenica I, Filipović V, Nuss JE, Gomba LM, Opsenica DM, Burnett JC, Gussio R, Šolaja BA, Bavari S. The synthesis of 2,5-bis(4-amidinophenyl)thiophene derivatives providing submicromolar-range inhibition of the botulinum neurotoxin serotype A metalloprotease. in European Journal of Medicinal Chemistry. 2012;53:374-379.
doi:10.1016/j.ejmech.2012.03.043 .

Opsenica, Igor, Filipović, Vuk, Nuss, Jon E., Gomba, Laura M., Opsenica, Dejan M., Burnett, James C., Gussio, Rick, Šolaja, Bogdan A., Bavari, Sina, "The synthesis of 2,5-bis(4-amidinophenyl)thiophene derivatives providing submicromolar-range inhibition of the botulinum neurotoxin serotype A metalloprotease" in European Journal of Medicinal Chemistry, 53 (2012):374-379,
https://doi.org/10.1016/j.ejmech.2012.03.043 . .

TY  - JOUR
AU  - Opsenica, Igor
AU  - Filipović, Vuk
AU  - Nuss, Jon E.
AU  - Gomba, Laura M.
AU  - Opsenica, Dejan M.
AU  - Burnett, James C.
AU  - Gussio, Rick
AU  - Šolaja, Bogdan A.
AU  - Bavari, Sina
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2787
AB  - Botulinum neurotoxins (BoNTs), composed of a family of seven serotypes (categorized A-G), are the deadliest of known biological toxins. The activity of the metalloprotease, light chain (LC) component of the toxins is responsible for causing the life-threatening paralysis associated with the disease botulism. Herein we report significantly more potent analogs of novel, lead BoNT serotype A LC inhibitor 2,5-bis(4-amidinophenyl)thiophene (K-i = 10.881 mu M +/- 0.90 mu M). Specifically, synthetic modifications involved simultaneously replacing the lead inhibitor's terminal bis-amidines with secondary amines and the systematic tethering of 4-amino-7-chloroquinoline substituents to provide derivatives with K-i values ranging from 0.302 mu M (+/- 0.03 mu M) to 0.889 mu M (+/- 0.11 mu M). (C) 2012 Elsevier Masson SAS. All rights reserved.
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Paris
T2  - European Journal of Medicinal Chemistry
T1  - The synthesis of 2,5-bis(4-amidinophenyl)thiophene derivatives providing submicromolar-range inhibition of the botulinum neurotoxin serotype A metalloprotease
VL  - 53
SP  - 374
EP  - 379
DO  - 10.1016/j.ejmech.2012.03.043
ER  - 

@article{
author = "Opsenica, Igor and Filipović, Vuk and Nuss, Jon E. and Gomba, Laura M. and Opsenica, Dejan M. and Burnett, James C. and Gussio, Rick and Šolaja, Bogdan A. and Bavari, Sina",
year = "2012",
abstract = "Botulinum neurotoxins (BoNTs), composed of a family of seven serotypes (categorized A-G), are the deadliest of known biological toxins. The activity of the metalloprotease, light chain (LC) component of the toxins is responsible for causing the life-threatening paralysis associated with the disease botulism. Herein we report significantly more potent analogs of novel, lead BoNT serotype A LC inhibitor 2,5-bis(4-amidinophenyl)thiophene (K-i = 10.881 mu M +/- 0.90 mu M). Specifically, synthetic modifications involved simultaneously replacing the lead inhibitor's terminal bis-amidines with secondary amines and the systematic tethering of 4-amino-7-chloroquinoline substituents to provide derivatives with K-i values ranging from 0.302 mu M (+/- 0.03 mu M) to 0.889 mu M (+/- 0.11 mu M). (C) 2012 Elsevier Masson SAS. All rights reserved.",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Paris",
journal = "European Journal of Medicinal Chemistry",
title = "The synthesis of 2,5-bis(4-amidinophenyl)thiophene derivatives providing submicromolar-range inhibition of the botulinum neurotoxin serotype A metalloprotease",
volume = "53",
pages = "374-379",
doi = "10.1016/j.ejmech.2012.03.043"
}

Opsenica, I., Filipović, V., Nuss, J. E., Gomba, L. M., Opsenica, D. M., Burnett, J. C., Gussio, R., Šolaja, B. A.,& Bavari, S.. (2012). The synthesis of 2,5-bis(4-amidinophenyl)thiophene derivatives providing submicromolar-range inhibition of the botulinum neurotoxin serotype A metalloprotease. in European Journal of Medicinal Chemistry
Elsevier France-Editions Scientifiques Medicales Elsevier, Paris., 53, 374-379.
https://doi.org/10.1016/j.ejmech.2012.03.043

Opsenica I, Filipović V, Nuss JE, Gomba LM, Opsenica DM, Burnett JC, Gussio R, Šolaja BA, Bavari S. The synthesis of 2,5-bis(4-amidinophenyl)thiophene derivatives providing submicromolar-range inhibition of the botulinum neurotoxin serotype A metalloprotease. in European Journal of Medicinal Chemistry. 2012;53:374-379.
doi:10.1016/j.ejmech.2012.03.043 .

Opsenica, Igor, Filipović, Vuk, Nuss, Jon E., Gomba, Laura M., Opsenica, Dejan M., Burnett, James C., Gussio, Rick, Šolaja, Bogdan A., Bavari, Sina, "The synthesis of 2,5-bis(4-amidinophenyl)thiophene derivatives providing submicromolar-range inhibition of the botulinum neurotoxin serotype A metalloprotease" in European Journal of Medicinal Chemistry, 53 (2012):374-379,
https://doi.org/10.1016/j.ejmech.2012.03.043 . .