TY  - JOUR
AU  - Borozan, Sunčica
AU  - Zlatović, Mario V.
AU  - Stojanović, Srđan
PY  - 2016
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/1387
AB  - We analyzed the potential influence of anion-pi interactions on the stability of complexes of proteins and halogen-containing non-natural amino acids. Anion-pi interactions are distance and orientation dependent and our ab initio calculations showed that their energy can be lower than -8 kcal mol(-1), while most of their interaction energies lie in the range from -1 to -4 kcal mol(-1). About 20 % of these interactions were found to be repulsive. We have observed that Tyr has the highest occurrence among the aromatic residues involved in anion-pi interactions, while His made the least contribution. Furthermore, our study showed that 67 % of total interactions in the dataset are multiple anion-pi interactions. Most of the amino acid residues involved in anion-pi interactions tend to be buried in the solvent-excluded environment. The majority of the anion-pi interacting residues are located in regions with helical secondary structure. Analysis of stabilization centers for these complexes showed that all of the six residues capable of anion-pi interactions are important in locating one or more of such centers. We found that anion-pi interacting residues are sometimes involved in simultaneous interactions with halogens as well. With all that in mind, we can conclude that the anion-pi interactions can show significant influence on molecular organization and on the structural stability of the complexes of proteins and halogen-containing non-natural amino acids. Their influence should not be neglected in supramolecular chemistry and crystal engineering fields as well.
PB  - Springer, New York
T2  - Journal of Biological Inorganic Chemistry
T1  - Anion-pi interactions in complexes of proteins and halogen-containing amino acids
VL  - 21
IS  - 3
SP  - 357
EP  - 368
DO  - 10.1007/s00775-016-1346-y
ER  - 

@article{
author = "Borozan, Sunčica and Zlatović, Mario V. and Stojanović, Srđan",
year = "2016",
abstract = "We analyzed the potential influence of anion-pi interactions on the stability of complexes of proteins and halogen-containing non-natural amino acids. Anion-pi interactions are distance and orientation dependent and our ab initio calculations showed that their energy can be lower than -8 kcal mol(-1), while most of their interaction energies lie in the range from -1 to -4 kcal mol(-1). About 20 % of these interactions were found to be repulsive. We have observed that Tyr has the highest occurrence among the aromatic residues involved in anion-pi interactions, while His made the least contribution. Furthermore, our study showed that 67 % of total interactions in the dataset are multiple anion-pi interactions. Most of the amino acid residues involved in anion-pi interactions tend to be buried in the solvent-excluded environment. The majority of the anion-pi interacting residues are located in regions with helical secondary structure. Analysis of stabilization centers for these complexes showed that all of the six residues capable of anion-pi interactions are important in locating one or more of such centers. We found that anion-pi interacting residues are sometimes involved in simultaneous interactions with halogens as well. With all that in mind, we can conclude that the anion-pi interactions can show significant influence on molecular organization and on the structural stability of the complexes of proteins and halogen-containing non-natural amino acids. Their influence should not be neglected in supramolecular chemistry and crystal engineering fields as well.",
publisher = "Springer, New York",
journal = "Journal of Biological Inorganic Chemistry",
title = "Anion-pi interactions in complexes of proteins and halogen-containing amino acids",
volume = "21",
number = "3",
pages = "357-368",
doi = "10.1007/s00775-016-1346-y"
}

Borozan, S., Zlatović, M. V.,& Stojanović, S.. (2016). Anion-pi interactions in complexes of proteins and halogen-containing amino acids. in Journal of Biological Inorganic Chemistry
Springer, New York., 21(3), 357-368.
https://doi.org/10.1007/s00775-016-1346-y

Borozan S, Zlatović MV, Stojanović S. Anion-pi interactions in complexes of proteins and halogen-containing amino acids. in Journal of Biological Inorganic Chemistry. 2016;21(3):357-368.
doi:10.1007/s00775-016-1346-y .

Borozan, Sunčica, Zlatović, Mario V., Stojanović, Srđan, "Anion-pi interactions in complexes of proteins and halogen-containing amino acids" in Journal of Biological Inorganic Chemistry, 21, no. 3 (2016):357-368,
https://doi.org/10.1007/s00775-016-1346-y . .

TY  - JOUR
AU  - Zlatović, Mario V.
AU  - Borozan, Sunčica
AU  - Nikolić, Milan R.
AU  - Stojanović, Srđan
PY  - 2015
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/1194
AB  - In this work, we have analyzed the influence of anion-pi interactions on the stability of high resolution protein-porphyrin complex crystal structures. The anion-pi interactions are distance and orientation dependent. Results of ab initio calculations of stabilization energies showed that they lie mostly in the range from -2 to -4 kcal mol(-1) with some of the anion-pi interactions having stabilization energies of up to -16 kcal mol(-1). In the anionic group, the numbers of anion-pi interactions involving Asp and Glu are similar, while His is more often involved in these interactions than other aromatic residues. Furthermore, our study showed that in the dataset used about 70% of the investigated anion-pi interactions are in fact multiple anion-pi interactions. Our results suggest that interacting residues are predominantly located in buried and partially buried regions. The secondary structure of the anion-pi interaction involving residues shows that most of the interacting residues preferred to be in helix conformations. Significant numbers of aromatic residues involved in anion-pi interactions have one or more stabilization centers, providing additional stability to the protein-porphyrin complexes. The conservation patterns indicate that more than half of the residues involved in these interactions are evolutionarily conserved, indicating that the contribution of the anion-pi interaction is an important factor for the structural stability of the investigated protein-porphyrin complexes.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Anion-pi interactions in protein-porphyrin complexes
VL  - 5
IS  - 48
SP  - 38361
EP  - 38372
DO  - 10.1039/c5ra03373j
ER  - 

@article{
author = "Zlatović, Mario V. and Borozan, Sunčica and Nikolić, Milan R. and Stojanović, Srđan",
year = "2015",
abstract = "In this work, we have analyzed the influence of anion-pi interactions on the stability of high resolution protein-porphyrin complex crystal structures. The anion-pi interactions are distance and orientation dependent. Results of ab initio calculations of stabilization energies showed that they lie mostly in the range from -2 to -4 kcal mol(-1) with some of the anion-pi interactions having stabilization energies of up to -16 kcal mol(-1). In the anionic group, the numbers of anion-pi interactions involving Asp and Glu are similar, while His is more often involved in these interactions than other aromatic residues. Furthermore, our study showed that in the dataset used about 70% of the investigated anion-pi interactions are in fact multiple anion-pi interactions. Our results suggest that interacting residues are predominantly located in buried and partially buried regions. The secondary structure of the anion-pi interaction involving residues shows that most of the interacting residues preferred to be in helix conformations. Significant numbers of aromatic residues involved in anion-pi interactions have one or more stabilization centers, providing additional stability to the protein-porphyrin complexes. The conservation patterns indicate that more than half of the residues involved in these interactions are evolutionarily conserved, indicating that the contribution of the anion-pi interaction is an important factor for the structural stability of the investigated protein-porphyrin complexes.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Anion-pi interactions in protein-porphyrin complexes",
volume = "5",
number = "48",
pages = "38361-38372",
doi = "10.1039/c5ra03373j"
}

Zlatović, M. V., Borozan, S., Nikolić, M. R.,& Stojanović, S.. (2015). Anion-pi interactions in protein-porphyrin complexes. in RSC Advances
Royal Soc Chemistry, Cambridge., 5(48), 38361-38372.
https://doi.org/10.1039/c5ra03373j

Zlatović MV, Borozan S, Nikolić MR, Stojanović S. Anion-pi interactions in protein-porphyrin complexes. in RSC Advances. 2015;5(48):38361-38372.
doi:10.1039/c5ra03373j .

Zlatović, Mario V., Borozan, Sunčica, Nikolić, Milan R., Stojanović, Srđan, "Anion-pi interactions in protein-porphyrin complexes" in RSC Advances, 5, no. 48 (2015):38361-38372,
https://doi.org/10.1039/c5ra03373j . .