Effect of amino acid substitution in the hydrophobic face of amphiphilic peptides on membrane curvature and perturbation: N‐terminal helix derived from adenovirus internal protein VI as a model
Effect of amino acid substitution in the hydrophobic face of amphiphilic peptides on membrane curvature and perturbation: N‐terminal helix derived from adenovirus internal protein VI as a model
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两亲肽疏水面氨基酸取代对膜曲率和扰动的影响:以腺病毒内部蛋白 VI 衍生的 N 端螺旋为模型
DOI:
10.1002/bip.22797
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发表时间:
2016
期刊:
影响因子:
2.4
通讯作者:
S. Futaki
中科院分区:
文献类型:
--
作者:
T. Murayama;S. Pujals;Hisaaki Hirose;I. Nakase;S. Futaki
The N‐terminal amphipathic helical segment of adenovirus internal protein VI (AdVpVI) plays a critical role in viral infection. Here, we report that the peptide segment corresponding to AdVpVI (positions 33–55) can induce positive membrane curvature together with membrane perturbation. The enhanced perturbation ability of the peptide was observed for membranes containing negatively charged phospholipids. Based on the liposome leakage assay, substitution of leucine at position 40 to other aliphatic (isoleucine) and aromatic (phenylalanine and tryptophan) residues yielded a similar degree of membrane perturbation by the peptides, which was considerably diminished by the substitution to glutamine. Further studies using the wild‐type AdVpVI (33–55) (WT) and phenylalanine‐substituted peptides (L40F) demonstrated that both peptides have positive membrane‐curvature‐inducing ability. These peptides showed higher binding affinity to 50‐nm large unilamellar vesicles (LUVs) than to 200‐nm LUVs. However, no enhanced perturbation by these peptides was observed for 50‐nm LUVs compared to 200‐nm LUVs, suggesting that both the original membrane curvature and the additional strain due to peptide insertion affect the membrane perturbation ability of these peptides. In the case of L40F, this peptide rather had a lower membrane perturbation ability for 50‐nm LUVs than for 200‐nm LUVs, which can be attributed to possible shallower binding of L40F on membranes. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 430–439, 2016.
影响因子:
3.4
作者:
Thennarasu, Sathiah;Tan, Anmin;Ramamoorthy, Ayyalusamy
通讯作者:
Ramamoorthy, Ayyalusamy
影响因子:
3.4
作者:
Reshetnyak, Yana K.;Segala, Michael;Engelman, Donald M.
通讯作者:
Engelman, Donald M.
影响因子:
3.4
作者:
Hallock, KJ;Lee, DK;Ramamoorthy, A
通讯作者:
Ramamoorthy, A