Mechanism of Reversible Peptide-Bilayer Attachment: Combined Simulation and Experimental Single-Molecule Study.
Mechanism of Reversible Peptide-Bilayer Attachment: Combined Simulation and Experimental Single-Molecule Study.
复制标题
可逆肽双层附着机制：模拟与实验单分子研究相结合。
作者：
N. Schwierz;S. Krysiak;T. Hugel;M. Zacharias
肽和蛋白质与脂质膜表面的结合对于许多膜介导的细胞过程是至关重要的。使用紧密匹配的分子动力学模拟和原子力显微镜实验，我们研究了力诱导的单肽链从磷脂双分子层的解吸，以获得微观上的洞察机制的可逆连接。这种方法允许量化的解吸力和分解成能量和熵的贡献肽膜相互作用。在模拟和实验中，具有带电和极性侧链的肽的解吸力比疏水肽的解吸力小得多。带电/极性肽吸附到膜表面是不利的高能成分，需要打破涉及肽的氢键，并有利于只有轻微的熵。相比之下，疏水肽的较强的吸附是有利于通过能量和熵和解吸力增加侧链的疏水性。有趣的是，计算出的净吸附自由能每个残留物与实验结果的单一残留物，表明侧链自由能的贡献在很大程度上是添加剂。这一观察结果可以帮助设计具有定制吸附特性的肽，并估计外周膜蛋白的膜结合特性。
The binding of peptides and proteins to lipid membrane surfaces is of fundamental importance for many membrane-mediated cellular processes. Using closely matched molecular dynamics simulations and atomic force microscopy experiments, we study the force-induced desorption of single peptide chains from phospholipid bilayers to gain microscopic insight into the mechanism of reversible attachment. This approach allows quantification of desorption forces and decomposition of peptide-membrane interactions into energetic and entropic contributions. In both simulations and experiments, the desorption forces of peptides with charged and polar side chains are much smaller than those for hydrophobic peptides. The adsorption of charged/polar peptides to the membrane surface is disfavored by the energetic components, requires breaking of hydrogen bonds involving the peptides, and is favored only slightly by entropy. By contrast, the stronger adsorption of hydrophobic peptides is favored both by energy and by entropy and the desorption forces increase with increasing side-chain hydrophobicity. Interestingly, the calculated net adsorption free energies per residue correlate with experimental results of single residues, indicating that side-chain free energy contributions are largely additive. This observation can help in the design of peptides with tailored adsorption properties and in the estimation of membrane binding properties of peripheral membrane proteins.
登录
查看更多内容
DOI：
10.1021/jz200167q
发表时间：
2011
期刊：
The journal of physical chemistry letters
影响因子：
--
作者：
Pastor RW;Mackerell AD Jr
通讯作者：
Mackerell AD Jr
影响因子：
3.3
作者：
Klauda, Jeffery B.;Venable, Richard M.;Freites, J. Alfredo;O'Connor, Joseph W.;Tobias, Douglas J.;Mondragon-Ramirez, Carlos;Vorobyov, Igor;MacKerell, Alexander D., Jr.;Pastor, Richard W.
通讯作者：
Pastor, Richard W.
影响因子：
3.4
作者：
Pan, Jianjun;Tristram-Nagle, Stephanie;Nagle, John F.
通讯作者：
Nagle, John F.
影响因子：
3.4
作者：
Evans, E;Ritchie, K
通讯作者：
Ritchie, K
DOI：
10.1016/s0304-4157(98)00021-5
发表时间：
1998-11-10
期刊：
BIOCHIMICA ET BIOPHYSICA ACTA-REVIEWS ON BIOMEMBRANES
影响因子：
--
作者：
White, SH;Wimley, WC
通讯作者：
Wimley, WC