Nettey-Oppong Ezekiel Edward, Muhammad Riaz, Ali Ahmed, Jeong Hyun-Woo, Seok Young-Seek, Kim Seong-Wan, Choi Seung Ho
Department of Biomedical Engineering, Yonsei University, Wonju 26493, Republic of Korea.
Department of Electrical Engineering, Sukkur IBA University, Sukkur 65200, Pakistan.
Materials (Basel). 2024 Nov 21;17(23):5686. doi: 10.3390/ma17235686.
silk fibroin is a promising biopolymer with notable mechanical strength, biocompatibility, and potential for diverse biomedical applications, such as tissue engineering scaffolds, and drug delivery. These properties are intrinsically linked to the structural characteristics of silk fibroin, making it essential to understand its molecular stability under varying environmental conditions. This study employed molecular dynamics simulations to examine the structural stability of silk I and silk II conformations of silk fibroin under changes in temperature (298 K to 378 K) and pressure (0.1 MPa to 700 MPa). Key parameters, including Root Mean Square Deviation (RMSD), Root Mean Square Fluctuation (RMSF), and Radius of Gyration (R) were analyzed, along with non-bonded interactions such as van der Waals and electrostatic potential energy. Our findings demonstrate that both temperature and pressure exert a destabilizing effect on silk fibroin, with silk I exhibiting a higher susceptibility to destabilization compared to silk II. Additionally, pressure elevated the van der Waals energy in silk I, while temperature led to a reduction. In contrast, electrostatic potential energy remained unaffected by these environmental conditions, highlighting stable long-range interactions throughout the study. Silk II's tightly packed β-sheet structure offers greater resilience to environmental changes, while the more flexible α-helices in silk I make it more susceptible to structural perturbations. These findings provide valuable insights into the atomic-level behavior of silk fibroin, contributing to a deeper understanding of its potential for applications in environments where mechanical or thermal stress is a factor. The study underscores the importance of computational approaches in exploring protein stability and supports the continued development of silk fibroin for biomedical and engineering applications.
丝素蛋白是一种很有前景的生物聚合物，具有显著的机械强度、生物相容性以及在多种生物医学应用中的潜力，如组织工程支架和药物递送。这些特性与丝素蛋白的结构特征内在相关，因此了解其在不同环境条件下的分子稳定性至关重要。本研究采用分子动力学模拟来研究丝素蛋白的丝I和丝II构象在温度（298 K至378 K）和压力（0.1 MPa至700 MPa）变化下的结构稳定性。分析了包括均方根偏差（RMSD）、均方根波动（RMSF）和回转半径（R）等关键参数，以及范德华力和静电势能等非键相互作用。我们的研究结果表明，温度和压力都会对丝素蛋白产生去稳定作用，与丝II相比，丝I对去稳定作用更敏感。此外，压力使丝I中的范德华能升高，而温度导致其降低。相比之下，静电势能不受这些环境条件的影响，突出了整个研究过程中稳定的长程相互作用。丝II紧密堆积的β-折叠结构对环境变化具有更大的弹性，而丝I中更灵活的α-螺旋使其更容易受到结构扰动。这些发现为丝素蛋白的原子水平行为提供了有价值的见解，有助于更深入地理解其在机械或热应力起作用的环境中的应用潜力。该研究强调了计算方法在探索蛋白质稳定性方面的重要性，并支持丝素蛋白在生物医学和工程应用中的持续发展。
