Dynamics of Protonated Peptide Ion Collisions with Organic Surfaces: Consonance of Simulation and Experiment
Dynamics of Protonated Peptide Ion Collisions with Organic Surfaces: Consonance of Simulation and Experiment
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DOI：
10.1021/acs.jpclett.6b00978
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发表时间：
2016-08-18
影响因子：
5.7
通讯作者：
Hase, William L.
中科院分区：
文献类型：
--
作者：
Pratihar, Subha;Barnes, George L.;Hase, William L.
在这个角度来看，质谱实验和化学动力学模拟已经探索了质子化的肽离子，肽-H+，与有机表面碰撞的原子动力学。这些研究已经调查了肽-H+表面诱导解离（SID），肽-H+在表面上的物理吸附，软着陆（SL），肽-H+与表面反应，反应着陆（RL）的能量传递和断裂动力学。SID提供了生物离子的初级结构和关于其碎裂途径和能量学的信息。两个SID机制被发现肽-H+断裂。一种传统的机制，其中肽-H+通过其与表面的碰撞而振动激发，从表面反弹，然后解离，这与统计RRKM单分子速率理论雅阁。另一种是粉碎，这是一种非统计机制，其中肽-H+在与表面碰撞时发生碎片，通过许多途径解离并形成许多产物离子。碎裂对于与金刚石和全氟化自组装单层（F-SAM）表面的碰撞是重要的，随着肽-H+碰撞能量的增加而增加。化学动力学模拟也提供了重要的机制上的SL和RL的生物离子表面的见解。模拟结果表明，SL发生通过多种机制组成的序列的肽-H+的物理吸附和渗透在表面上。SL和RL具有广泛的重要应用，包括蛋白质或肽微阵列的制备，生物相容性基底和生物传感器的开发，以及包括纳米材料在内的新型合成材料的制备。一个重要的RL机制是肽-H+在表面上的完整沉积。
In this Perspective, mass spectrometry experiments and chemical dynamics simulations are described that have explored the atomistic dynamics of protonated peptide ions, peptide-H+, colliding with organic surfaces. These studies have investigated the energy transfer and fragmentation dynamics for peptide-H+ surface-induced dissociation (SID), peptide-H+ physisorption on the surface, soft landing (SL), and peptide-H+ reaction with the surface, reactive landing (RL). SID provides primary structures of biological ions and information regarding their fragmentation pathways and energetics. Two SID mechanisms are found for peptide-H+ fragmentation. A traditional mechanism in which peptide-H+ is vibrationally excited by its collision with the surface, rebounds off the surface and then dissociates in accord with the statistical, RRKM unimolecular rate theory. The other, shattering, is a nonstatistical mechanism in which peptide-H+ fragments as it collides with the surface, dissociating via many pathways and forming many product ions. Shattering is important for collisions with diamond and perfluorinated self-assembled monolayer (F-SAM) surfaces, increasing in importance with the peptide-H+ collision energy. Chemical dynamics simulations also provide important mechanistic insights on SL and RL of biological ions on surfaces. The simulations indicate that SL occurs via multiple mechanisms consisting of sequences of peptide-H+ physisorption on and penetration in the surface. SL and RL have a broad range of important applications including preparation of protein or peptide microarrays, development of biocompatible substrates and biosensors, and preparation of novel synthetic materials, including nanomaterials. An important RL mechanism is intact deposition of peptide-H+ on the surface.