Molecular dynamics simulations of peptides at the air-water interface: influencing factors on peptide-templated mineralization.
Molecular dynamics simulations of peptides at the air-water interface: influencing factors on peptide-templated mineralization.
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空气-水界面肽的分子动力学模拟：肽模板矿化的影响因素
DOI：
10.1021/la503549q
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
C. Peter
中科院分区：
文献类型：
--
作者：
A. Jain;M. Jochum;C. Peter
生物矿化是一个复杂的、与生物医学高度相关的过程，生物体通过该过程将矿物质沉积在生物基质上，以硬化组织并构建骨骼结构和外壳。 Rapaport 及其同事（J. Am. Chem. Soc. 2000, 122, 12523；Adv. Funct. Mater. 2008, 18, 2889；Acta Biomater. 2012, 8, 2466）设计了一类自组装两亲性肽，它们能够形成水凝胶并吸引环境中的离子，生成类似的结构细胞外基质并促进骨再生。空气-水界面在实验和模拟中用作模型疏水表面，以模拟细胞的有机-水界面，并研究肽基质组织成有序的 β 折叠单层以及随后生物矿物质形成的开始。为了深入了解潜在的分子机制，我们使用分子动力学模拟来研究肽序列对聚集体稳定性和离子-肽相互作用的影响。我们发现，与实验观察结果非常一致，肽末端的性质（脯氨酸与苯丙氨酸）影响聚集体的顺序，而酸性侧链（天冬氨酸与谷氨酸）的性质影响聚集体在离子存在下的稳定性。这些模拟为了解离子和肽模板在成核之前生物矿化的早期阶段相互影响的方式提供了有价值的微观见解。
Biomineralization is the intricate, biomedically highly relevant process by which living organisms deposit minerals on biological matrices to stiffen tissues and build skeletal structures and shells. Rapaport and coworkers (J. Am. Chem. Soc. 2000, 122, 12523; Adv. Funct. Mater. 2008, 18, 2889; Acta Biomater. 2012, 8, 2466) have designed a class of self-assembling amphiphilic peptides that are capable of forming hydrogels and attracting ions from the environment, generating structures akin to the extracellular matrix and promoting bone regeneration. The air–water interface serves both in experiment and in simulations as a model hydrophobic surface to mimic the cell’s organic–aqueous interface and to investigate the organization of the peptide matrix into ordered β-pleated monolayers and the subsequent onset of biomineral formation. To obtain insight into the underlying molecular mechanism, we have used molecular dynamics simulations to study the effect of peptide sequence on aggregate stability and ion–peptide interactions. We findin excellent agreement with experimental observationsthat the nature of the peptide termini (proline vs phenylalanine) affect the aggregate order, while the nature of the acidic side chains (aspartic vs glutamic acid) affect the aggregate’s stability in the presence of ions. These simulations provide valuable microscopic insight into the way ions and peptide templates mutually affect each other during the early stages of biomineralization preceding nucleation.
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影响因子：
--
作者：
Shan-Lai Zhou;S. Matsumoto;Hua Tian;Hiroki Yamane;A. Ojida;Shigeki Kiyonaka;I. Hamachi
通讯作者：
Shan-Lai Zhou;S. Matsumoto;Hua Tian;Hiroki Yamane;A. Ojida;Shigeki Kiyonaka;I. Hamachi
影响因子：
19
作者：
Rapaport, Hanna;Grisaru, Haviv;Silberstein, Tova
通讯作者：
Silberstein, Tova
DOI：
10.1073/pnas.0407273101
发表时间：
2004-11-16
影响因子：
11.1
作者：
Nguyen, HD;Hall, CK
通讯作者：
Hall, CK
影响因子：
62.1
作者：
Palmer, Liam C.;Newcomb, Christina J.;Kaltz, Stuart R.;Spoerke, Erik D.;Stupp, Samuel I.
通讯作者：
Stupp, Samuel I.
影响因子：
3.3
作者：
Segman-Magidovich, Shlomit;Rapaport, Hanna
通讯作者：
Rapaport, Hanna