Burguera Sergi, Vidal Lenin, Bauzá Antonio
Department of Chemistry, Universitat de les Illes Balears, Ctra. de Valldemossa, km. 7.5, 07122, Palma de Mallorca, Islas Baleares, Spain.
Chempluschem. 2025 Jan;90(1):e202400578. doi: 10.1002/cplu.202400578. Epub 2024 Nov 7.
The Protein Data Bank (PDB) was scrutinized for the presence of noncovalent O ⋅ ⋅ ⋅ Al Triel Bonding (TrB) interactions, involving protein residues (e. g. GLU and GLN), adenosine/guanine diphosphate moieties (ADP and GDP), water molecules and two aluminum fluorides (AlF and AlF ). The results were statistically analyzed, revealing a vast number of O ⋅ ⋅ ⋅ Al contacts in the active sites of phosphoryl transfer enzymes, with a marked directionality towards the Al σ-/π-hole. The physical nature of the TrBs studied herein was analyzed using Molecular Electrostatic Potential (MEP) maps, the Quantum Theory of Atoms in Molecules (QTAIM), the Non Covalent Interaction plot (NCIplot) visual index and Natural Bonding Orbital (NBO) studies. As far as our knowledge extends, it is the first time that O ⋅ ⋅ ⋅ Al TrBs are analyzed within a biological context, participating in protein trapping mechanisms related to phosphoryl transfer enzymes. Moreover, since they are involved in the stabilization of aluminum fluorides inside the protein's active site, we believe the results reported herein will be valuable for those scientists working in supramolecular chemistry, catalysis and rational drug design.
对蛋白质数据库（PDB）进行了审查，以查找是否存在非共价O⋅⋅⋅Al三中心键合（TrB）相互作用，这些相互作用涉及蛋白质残基（例如GLU和GLN）、腺苷/鸟苷二磷酸部分（ADP和GDP）、水分子以及两个氟化铝（AlF和AlF）。对结果进行了统计分析，发现在磷酸转移酶的活性位点存在大量的O⋅⋅⋅Al接触，且明显朝着Al的σ-/π-空穴方向。本文使用分子静电势（MEP）图、分子中的原子量子理论（QTAIM）、非共价相互作用图（NCIplot）可视化指标和自然键轨道（NBO）研究对所研究的TrB的物理性质进行了分析。就我们所知，这是首次在生物学背景下分析O⋅⋅⋅Al TrB，其参与了与磷酸转移酶相关的蛋白质捕获机制。此外，由于它们参与了蛋白质活性位点内氟化铝的稳定化，我们相信本文报道的结果将对从事超分子化学、催化和合理药物设计的科学家有价值。
