Grupo de Investigación en Química Teórica y Experimental (QUITEX), Departamento de Ingeniería Química, Universidad Tecnológica Nacional, Facultad Regional Resistencia, French 414 (H3500CHJ), Resistencia, Chaco, Argentina; Instituto de Química Básica y Aplicada del Nordeste Argentino, IQUIBA-NEA, UNNE-CONICET, Avenida Libertad 5460, 3400 Corrientes, Argentina.
Grupo de Investigación en Química Teórica y Experimental (QUITEX), Departamento de Ingeniería Química, Universidad Tecnológica Nacional, Facultad Regional Resistencia, French 414 (H3500CHJ), Resistencia, Chaco, Argentina.
Biophys Chem. 2021 Sep;276:106627. doi: 10.1016/j.bpc.2021.106627. Epub 2021 May 29.
Molecular interactions between proteins and polyphenols are responsible for many natural phenomena like colloidal turbidity, astringency, denaturation of enzymes and leather tanning. Although these phenomena are well known, there are open questions about the specific interactions involved in the complexation process. In this work, Molecular Dynamic (MD) simulations and the topology of the electron density analysis were used to study the interactions between the flavonoid procyanidin C1 and a collagen fragment solvated in water. Root mean square deviation; root mean square fluctuation and hydrogen bonds occupancy were examined after 50 ns. The interactions were also analyzed by means of the quantum theory of atoms in molecules. Our results show that the main interactions are hydrogen bonds between -OH groups of the polyphenol and CO groups of the peptide bond. Stacking interactions between proline rings and phenol rings, that is CH⋯π hydrogen bonds, also stabilize the dynamic structure of the complex.
蛋白质和多酚之间的分子相互作用是许多自然现象的原因，如胶体浑浊、收敛性、酶变性和皮革鞣制。尽管这些现象是众所周知的，但对于复杂过程中涉及的特定相互作用仍存在一些问题。在这项工作中，使用分子动力学（MD）模拟和电子密度拓扑分析研究了在水中溶解的类黄酮原花青素 C1 与胶原片段之间的相互作用。在 50ns 后检查均方根偏差；均方根波动和氢键占有率。还通过原子在分子中的量子理论分析了相互作用。我们的结果表明，主要相互作用是多酚的-OH 基团与肽键的 CO 基团之间的氢键。脯氨酸环和苯酚环之间的堆积相互作用，即 CH⋯π 氢键，也稳定了复合物的动态结构。
