KRSR 肽与二氧化钛锐钛矿 (100) 表面的相互作用：分子动力学模拟研究,International Journal of Molecular Sciences

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KRSR 肽与二氧化钛锐钛矿 (100) 表面的相互作用：分子动力学模拟研究
International Journal of Molecular Sciences ( IF 4.9 ) Pub Date : 2021-12-09 , DOI: 10.3390/ijms222413251
Tamás Tarjányi ₁ , Ferenc Bogár ₂ , Janos Minarovits ₁ , Márió Gajdács ₁ , Zsolt Tóth ₃

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由于其抗拉强度和优异的生物相容性，钛 (Ti) 通常用作医学和牙科中的植入材料。牙种植体的成功取决于钛种植体的氧化表面与周围骨组织之间形成的接触。蛋白质和肽对植入物表面的吸附允许成骨成骨细胞粘附到这种修饰的表面上。最近，已经观察到四肽 KRSR (Lys-Arg-Ser-Arg) 功能化可以促进成骨细胞粘附到植入物表面。这可以促进建立有效的骨与植入物接触并提高愈合过程中的植入物稳定性。GROMACS 是一种分子动力学软件包，用于执行 200 ns 模拟 KRSR 肽对 TiO2 的吸附₂（锐钛矿）表面在水性环境中。分子构象用复制交换分子动力学 (REMD) 模拟进行映射，以评估锐钛矿表面上可能的肽构象，并使用伞形采样方法计算最常见构象的结合能。模拟表明，KRSR 肽迁移并以稳定的位置附着在表面上。_{与 TiO 2}相互作用的主要氨基酸残基表面是 N 端带电荷的赖氨酸 (K) 残基。REMD 表明 KRSR 肽具有独特的构象。在这种构象中，表面仅与赖氨酸残基相互作用，而 ser (S) 和 arg (R) 残基与远离表面的水分子相互作用。KRSR肽最常见构象与锐钛矿（100）表面的结合自由能为ΔG = -8.817 kcal/mol。_{我们的结果表明，N-末端赖氨酸残基在 KRSR 与 TiO 2}表面的粘附中起重要作用，并可能影响牙种植体的骨整合。

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Interaction of KRSR Peptide with Titanium Dioxide Anatase (100) Surface: A Molecular Dynamics Simulation Study

Due to its tensile strength and excellent biocompatibility, titanium (Ti) is commonly used as an implant material in medicine and dentistry. The success of dental implants depends on the formation of a contact between the oxidized surface of Ti implant and the surrounding bone tissue. The adsorption of proteins and peptides to the implant surface allows the bone-forming osteoblast cells to adhere to such modified surfaces. Recently, it has been observed that tetrapeptide KRSR (Lys-Arg-Ser-Arg) functionalization could promote osteoblast adhesion to implant surfaces. This may facilitate the establishment of an efficient bone-to implant contact and improve implant stability during the healing process. GROMACS, a molecular dynamics software package was used to perform a 200 ns simulation of adsorption of the KRSR peptide to the TiO₂ (anatase) surface in an aqueous environment. The molecule conformations were mapped with Replica Exchange Molecular Dynamics (REMD) simulations to assess the possible peptide conformations on the anatase surface, and the umbrella sampling method was used to calculate the binding energy of the most common conformation. The simulations have shown that the KRSR peptide migrates and attaches to the surface in a stable position. The dominant amino acid residue interacting with the TiO₂ surface was the N-terminal charged lysine (K) residue. REMD indicated that there is a distinct conformation that is taken by the KRSR peptide. In this conformation the surface interacts only with the lysine residue while the ser (S) and arg (R) residues interact with water molecules farther from the surface. The binding free energy of the most common conformation of KRSR peptide to the anatase (100) surface was ΔG = −8.817 kcal/mol. Our result suggests that the N-terminal lysine residue plays an important role in the adhesion of KRSR to the TiO₂ surface and may influence the osseointegration of dental implants.

更新日期：2021-12-09

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