Backbone Structure of Diatom Silaffin Peptide R5 in Biosilica Determined by Combining Solid-State NMR with Theoretical Sum-Frequency Generation Spectra.
Backbone Structure of Diatom Silaffin Peptide R5 in Biosilica Determined by Combining Solid-State NMR with Theoretical Sum-Frequency Generation Spectra.
复制标题
通过结合固态 NMR 与理论和频生成光谱测定生物二氧化硅中硅藻硅蜡肽 R5 的主链结构。
DOI：
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发表时间：
2021
影响因子：
5.7
通讯作者：
T. Weidner
中科院分区：
文献类型：
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作者：
Steven Joop Roeters;R. Mertig;Helmut Lutz;Adrienne M. Roehrich;G. Drobny;T. Weidner
Silaffin肽R5是硅藻二氧化硅细胞壁生物发生的关键。R5肽的生物硅化在生物技术、药物开发和材料科学中具有潜力，因为它能够沉淀稳定、高保真的二氧化硅片和颗粒。设计用于更广泛应用的新型肽基结构的真正障碍是对沉淀二氧化硅纳米颗粒时R5的界面结构的有限理解。虽然R5-二氧化硅相互作用已经在平坦表面上进行了详细研究，但纳米颗粒内的结构仍在争论中。我们在此阐明的构象R5在其活性形式内的二氧化硅颗粒结合界面特定的振动光谱数据与固态NMR扭转角，使用理论光谱。我们的计算表明，R5的结构，并经历了构象转变，从一个链型基序在解决方案中的一个更弯曲，收缩的结构时，与二氧化硅前体相互作用。
Silaffin peptide R5 is key for the biogenesis of silica cell walls of diatoms. Biosilification by the R5 peptide has potential in biotechnology, drug development, and materials science due to its ability to precipitate stable, high fidelity silica sheets and particles. A true barrier for the design of novel peptide-based architectures for wider applications has been the limited understanding of the interfacial structure of R5 when precipitating silica nanoparticles. While R5-silica interactions have been studied in detail at flat surfaces, the structure within nanophase particles is still being debated. We herein elucidate the conformation of R5 in its active form within silica particles by combining interface-specific vibrational spectroscopy data with solid-state NMR torsion angles using theoretical spectra. Our calculations show that R5 is structured and undergoes a conformational transition from a strand-type motif in solution to a more curved, contracted structure when interacting with silica precursors.
影响因子：
3.3
作者：
Nguyen, Khoi Tan;King, John Thomas;Chen, Zhan
通讯作者：
Chen, Zhan
影响因子：
15
作者：
Lu, Hao;Lutz, Helmut;Weidner, Tobias
通讯作者：
Weidner, Tobias
影响因子：
18.3
作者：
Adrienne M. Roehrich;G. Drobny
通讯作者：
Adrienne M. Roehrich;G. Drobny