Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study
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2022
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The influences of cation−π interactions in phycocyanin proteins and their environmental preferences were analyzed. The number of interactions formed by arginine showed to be higher than those formed by the lysine in the cationic group, while histidine is comparatively higher than phenylalanine and N-terminal residue in the π group. Arg−Tyr and Arg−Phe interacting pairs are predominant among the various pairs analyzed. Cation−π interactions are distance-dependent and can be realized above a wider area above the π ring. We analyzed the energy contribution resulting from cation−π interactions using ab initio calculations. The energy contribution resulting from the most frequent cation−π interactions was in the lower range of strong hydrogen bonds. The results showed that, while most of their interaction energies lay ranged from − 2 to − 8 kcal/mol, those energies could be up to −12− 12 kcal/mol. Stabilization centers for these proteins showed that all residues found in cation−π interactio...ns are important in locating one or more of such centers. In the cation–π interacting residues, 54% of the amino acid residues involved in these interactions might be conserved in phycocyanins. From this study, we infer that cation−π forming residues play an important role in the stability of the multiply commercially used phycocyanin proteins and could help structural biologists and medicinal chemists to design better and safer drugs.
Ključne reči:
Ab initio study / Amino acid conservation / Cation-π interactions / Phycocyanin / Stabilization centersIzvor:
Computational Biology and Chemistry, 2022, 100, 107752Izdavač:
- Elsevier
Finansiranje / projekti:
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200026 (Univerzitet u Beogradu, Institut za hemiju, tehnologiju i metalurgiju - IHTM) (RS-MESTD-inst-2020-200026)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200168 (Univerzitet u Beogradu, Hemijski fakultet) (RS-MESTD-inst-2020-200168)
DOI: 10.1016/j.compbiolchem.2022.107752
ISSN: 1476-9271
PubMed: 35963077
Scopus: 2-s2.0-85135708127
Institucija/grupa
IHTMTY - JOUR AU - Breberina, Luka M. AU - Nikolić, Milan R. AU - Stojanović, Srđan AU - Zlatović, Mario PY - 2022 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/5330 AB - The influences of cation−π interactions in phycocyanin proteins and their environmental preferences were analyzed. The number of interactions formed by arginine showed to be higher than those formed by the lysine in the cationic group, while histidine is comparatively higher than phenylalanine and N-terminal residue in the π group. Arg−Tyr and Arg−Phe interacting pairs are predominant among the various pairs analyzed. Cation−π interactions are distance-dependent and can be realized above a wider area above the π ring. We analyzed the energy contribution resulting from cation−π interactions using ab initio calculations. The energy contribution resulting from the most frequent cation−π interactions was in the lower range of strong hydrogen bonds. The results showed that, while most of their interaction energies lay ranged from − 2 to − 8 kcal/mol, those energies could be up to −12− 12 kcal/mol. Stabilization centers for these proteins showed that all residues found in cation−π interactions are important in locating one or more of such centers. In the cation–π interacting residues, 54% of the amino acid residues involved in these interactions might be conserved in phycocyanins. From this study, we infer that cation−π forming residues play an important role in the stability of the multiply commercially used phycocyanin proteins and could help structural biologists and medicinal chemists to design better and safer drugs. PB - Elsevier T2 - Computational Biology and Chemistry T1 - Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study VL - 100 IS - 107752 DO - 10.1016/j.compbiolchem.2022.107752 ER -
@article{ author = "Breberina, Luka M. and Nikolić, Milan R. and Stojanović, Srđan and Zlatović, Mario", year = "2022", abstract = "The influences of cation−π interactions in phycocyanin proteins and their environmental preferences were analyzed. The number of interactions formed by arginine showed to be higher than those formed by the lysine in the cationic group, while histidine is comparatively higher than phenylalanine and N-terminal residue in the π group. Arg−Tyr and Arg−Phe interacting pairs are predominant among the various pairs analyzed. Cation−π interactions are distance-dependent and can be realized above a wider area above the π ring. We analyzed the energy contribution resulting from cation−π interactions using ab initio calculations. The energy contribution resulting from the most frequent cation−π interactions was in the lower range of strong hydrogen bonds. The results showed that, while most of their interaction energies lay ranged from − 2 to − 8 kcal/mol, those energies could be up to −12− 12 kcal/mol. Stabilization centers for these proteins showed that all residues found in cation−π interactions are important in locating one or more of such centers. In the cation–π interacting residues, 54% of the amino acid residues involved in these interactions might be conserved in phycocyanins. From this study, we infer that cation−π forming residues play an important role in the stability of the multiply commercially used phycocyanin proteins and could help structural biologists and medicinal chemists to design better and safer drugs.", publisher = "Elsevier", journal = "Computational Biology and Chemistry", title = "Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study", volume = "100", number = "107752", doi = "10.1016/j.compbiolchem.2022.107752" }
Breberina, L. M., Nikolić, M. R., Stojanović, S.,& Zlatović, M.. (2022). Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study. in Computational Biology and Chemistry Elsevier., 100(107752). https://doi.org/10.1016/j.compbiolchem.2022.107752
Breberina LM, Nikolić MR, Stojanović S, Zlatović M. Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study. in Computational Biology and Chemistry. 2022;100(107752). doi:10.1016/j.compbiolchem.2022.107752 .
Breberina, Luka M., Nikolić, Milan R., Stojanović, Srđan, Zlatović, Mario, "Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study" in Computational Biology and Chemistry, 100, no. 107752 (2022), https://doi.org/10.1016/j.compbiolchem.2022.107752 . .