TY  - JOUR
AU  - Micovic, Vuk
AU  - Ivanović, Milovan
AU  - Došen-Mićović, Ljiljana
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/872
AB  - An automated docking procedure was used to study binding of a series of delta-selective ligands to three models of the delta-opioid receptor. These models are thought to represent the three ligand-specific receptor conformations. Docking results are in agreement with point mutation studies and suggest that different ligands-agonists and antagonists-may bind to the same binding site under different receptor conformations. Docking to different receptor models ( conformations) also suggests that by changing to a receptor-specific conformation, the receptor may open or close different binding sites to other ligands.
PB  - Springer, New York
T2  - Journal of Molecular Modeling
T1  - Docking studies suggest ligand-specific delta-opioid receptor conformations
VL  - 15
IS  - 3
SP  - 267
EP  - 280
DO  - 10.1007/s00894-008-0396-7
ER  - 

@article{
author = "Micovic, Vuk and Ivanović, Milovan and Došen-Mićović, Ljiljana",
year = "2009",
abstract = "An automated docking procedure was used to study binding of a series of delta-selective ligands to three models of the delta-opioid receptor. These models are thought to represent the three ligand-specific receptor conformations. Docking results are in agreement with point mutation studies and suggest that different ligands-agonists and antagonists-may bind to the same binding site under different receptor conformations. Docking to different receptor models ( conformations) also suggests that by changing to a receptor-specific conformation, the receptor may open or close different binding sites to other ligands.",
publisher = "Springer, New York",
journal = "Journal of Molecular Modeling",
title = "Docking studies suggest ligand-specific delta-opioid receptor conformations",
volume = "15",
number = "3",
pages = "267-280",
doi = "10.1007/s00894-008-0396-7"
}

Micovic, V., Ivanović, M.,& Došen-Mićović, L.. (2009). Docking studies suggest ligand-specific delta-opioid receptor conformations. in Journal of Molecular Modeling
Springer, New York., 15(3), 267-280.
https://doi.org/10.1007/s00894-008-0396-7

Micovic V, Ivanović M, Došen-Mićović L. Docking studies suggest ligand-specific delta-opioid receptor conformations. in Journal of Molecular Modeling. 2009;15(3):267-280.
doi:10.1007/s00894-008-0396-7 .

Micovic, Vuk, Ivanović, Milovan, Došen-Mićović, Ljiljana, "Docking studies suggest ligand-specific delta-opioid receptor conformations" in Journal of Molecular Modeling, 15, no. 3 (2009):267-280,
https://doi.org/10.1007/s00894-008-0396-7 . .

TY  - JOUR
AU  - Dosen-Miovic, Ljiljana
AU  - Ivanović, Milovan
AU  - Micovic, Vuk
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/852
AB  - Fentanyl is a highly potent and clinically widely used narcotic analgesic. The synthesis of its analogs remains a challenge in an attempt to develop highly selective mu-opioid receptor agonists with specific pharmacological properties. In this paper, the use of flexible molecular docking of several specific fentanyl analogs to the mu-opioid receptor model, in order to test the hypothesis that the hydrophobic pocket accommodates alkyl groups at position 3 of the fentanyl skeleton, is described. The stereoisomers of the following compounds were studied: cis- and trans-3-methylfentanyl. 3.3-dimethylfentanyl. cis- and trans-3-ethylfentanyl, cis- and trans-3-propylfentanyl, cis-3-isopropylfentanyl and cis-3-benzylfentanyl. The optimal position and orientation of these fentanyl analogs in the binding pocket of the mu-receptor, explaining their enantiospecific potency, were determined. It was found that the 3-alkyl group of cis-3R,4S and trans-3S,4S stereoisomers of all the active compounds occupies the hydrophobic pocket between TM5, TM6 and TM7, made LIP of the amino acids Trp318 (TM7), Ile322 (TM7), 1001 (TM6) and Phe237 (TM5). However, the fact that this hydrophobic pocket can also accommodate the bulky 3-alkyl substituents of the two inactive Compounds: cis-3-isopropylfentanyl, and cis-3-benzylfentanyl, indicates that this hydrophobic pocket in the employed receptor model is probably too large.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Location of the hydrophobic pocket in the binding site of fentanyl analogs in the mu-opioid receptor
VL  - 72
IS  - 7
SP  - 643
EP  - 654
DO  - 10.2298/JSC0707643D
ER  - 

@article{
author = "Dosen-Miovic, Ljiljana and Ivanović, Milovan and Micovic, Vuk",
year = "2007",
abstract = "Fentanyl is a highly potent and clinically widely used narcotic analgesic. The synthesis of its analogs remains a challenge in an attempt to develop highly selective mu-opioid receptor agonists with specific pharmacological properties. In this paper, the use of flexible molecular docking of several specific fentanyl analogs to the mu-opioid receptor model, in order to test the hypothesis that the hydrophobic pocket accommodates alkyl groups at position 3 of the fentanyl skeleton, is described. The stereoisomers of the following compounds were studied: cis- and trans-3-methylfentanyl. 3.3-dimethylfentanyl. cis- and trans-3-ethylfentanyl, cis- and trans-3-propylfentanyl, cis-3-isopropylfentanyl and cis-3-benzylfentanyl. The optimal position and orientation of these fentanyl analogs in the binding pocket of the mu-receptor, explaining their enantiospecific potency, were determined. It was found that the 3-alkyl group of cis-3R,4S and trans-3S,4S stereoisomers of all the active compounds occupies the hydrophobic pocket between TM5, TM6 and TM7, made LIP of the amino acids Trp318 (TM7), Ile322 (TM7), 1001 (TM6) and Phe237 (TM5). However, the fact that this hydrophobic pocket can also accommodate the bulky 3-alkyl substituents of the two inactive Compounds: cis-3-isopropylfentanyl, and cis-3-benzylfentanyl, indicates that this hydrophobic pocket in the employed receptor model is probably too large.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Location of the hydrophobic pocket in the binding site of fentanyl analogs in the mu-opioid receptor",
volume = "72",
number = "7",
pages = "643-654",
doi = "10.2298/JSC0707643D"
}

Dosen-Miovic, L., Ivanović, M.,& Micovic, V.. (2007). Location of the hydrophobic pocket in the binding site of fentanyl analogs in the mu-opioid receptor. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 72(7), 643-654.
https://doi.org/10.2298/JSC0707643D

Dosen-Miovic L, Ivanović M, Micovic V. Location of the hydrophobic pocket in the binding site of fentanyl analogs in the mu-opioid receptor. in Journal of the Serbian Chemical Society. 2007;72(7):643-654.
doi:10.2298/JSC0707643D .

Dosen-Miovic, Ljiljana, Ivanović, Milovan, Micovic, Vuk, "Location of the hydrophobic pocket in the binding site of fentanyl analogs in the mu-opioid receptor" in Journal of the Serbian Chemical Society, 72, no. 7 (2007):643-654,
https://doi.org/10.2298/JSC0707643D . .

TY  - JOUR
AU  - Došen-Mićović, Ljiljana
AU  - Ivanović, Milovan
AU  - Micovic, V
PY  - 2006
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/771
AB  - Fentanyl is a highly potent and clinically widely used narcotic analgesic. The synthesis of its analogs remains a challenge in the attempt to develop highly selective p-opioid receptor agonists with specific pharmacological properties. In this paper, the use of flexible molecular docking in a Study of the formation of complexes between a series of active fentanyl analogs and the mu-opioid receptor is described. The optimal position and orientation Of fourteen fentanyl analogs in the binding pocket of the mu-receptor were determined. The major receptor amino acids and the ligand functional groups participating in the complex formation were identified. Stereochemical effects on the potency and binding are explained. The proposed model of ligand-receptor binding is in agreement with point mutation experiments explaining the role of the amino acids: Asp147, Tyr148, Asn230, His297, Trp318, His319, Cys321, and Tyr326 in the complex formation. In addition, the following amino acids were identified as being important for ligand binding or receptor activation: Ile322, Gly325, Val300, Met203, Leu200, Val143, and Ile144. (c) 2005 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Bioorganic and Medicinal Chemistry
T1  - Steric interactions and the activity of fentanyl analogs at the mu-opioid receptor
VL  - 14
IS  - 9
SP  - 2887
EP  - 2895
DO  - 10.1016/j.bmc.2005.12.010
ER  - 

@article{
author = "Došen-Mićović, Ljiljana and Ivanović, Milovan and Micovic, V",
year = "2006",
abstract = "Fentanyl is a highly potent and clinically widely used narcotic analgesic. The synthesis of its analogs remains a challenge in the attempt to develop highly selective p-opioid receptor agonists with specific pharmacological properties. In this paper, the use of flexible molecular docking in a Study of the formation of complexes between a series of active fentanyl analogs and the mu-opioid receptor is described. The optimal position and orientation Of fourteen fentanyl analogs in the binding pocket of the mu-receptor were determined. The major receptor amino acids and the ligand functional groups participating in the complex formation were identified. Stereochemical effects on the potency and binding are explained. The proposed model of ligand-receptor binding is in agreement with point mutation experiments explaining the role of the amino acids: Asp147, Tyr148, Asn230, His297, Trp318, His319, Cys321, and Tyr326 in the complex formation. In addition, the following amino acids were identified as being important for ligand binding or receptor activation: Ile322, Gly325, Val300, Met203, Leu200, Val143, and Ile144. (c) 2005 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Bioorganic and Medicinal Chemistry",
title = "Steric interactions and the activity of fentanyl analogs at the mu-opioid receptor",
volume = "14",
number = "9",
pages = "2887-2895",
doi = "10.1016/j.bmc.2005.12.010"
}

Došen-Mićović, L., Ivanović, M.,& Micovic, V.. (2006). Steric interactions and the activity of fentanyl analogs at the mu-opioid receptor. in Bioorganic and Medicinal Chemistry
Pergamon-Elsevier Science Ltd, Oxford., 14(9), 2887-2895.
https://doi.org/10.1016/j.bmc.2005.12.010

Došen-Mićović L, Ivanović M, Micovic V. Steric interactions and the activity of fentanyl analogs at the mu-opioid receptor. in Bioorganic and Medicinal Chemistry. 2006;14(9):2887-2895.
doi:10.1016/j.bmc.2005.12.010 .

Došen-Mićović, Ljiljana, Ivanović, Milovan, Micovic, V, "Steric interactions and the activity of fentanyl analogs at the mu-opioid receptor" in Bioorganic and Medicinal Chemistry, 14, no. 9 (2006):2887-2895,
https://doi.org/10.1016/j.bmc.2005.12.010 . .