Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2.
Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2.
复制标题
DOI：
10.1016/s0021-9258(18)48270-1
复制
发表时间：
1987-05
期刊：
影响因子：
--
通讯作者：
J. D. Lear;W. DeGrado
中科院分区：
文献类型：
--
作者：
J. D. Lear;W. DeGrado
合成肽代表氨基酸残基1-16和1-20，这是流感病毒血凝素HA-2亚基的一个拟议的融合区，与具有亚微摩尔解离常数的磷脂酰胆碱囊泡结合。1-20肽，而不是1-16肽，当与囊泡结合并协同促进囊泡融合时，似乎采用螺旋构象。
Synthetic peptides representing amino acid residues 1-16 and 1-20, a proposed fusogenic region of the HA-2 subunit of influenza virus hemagglutinin, bind to phosphatidylcholine vesicles with submicromolar dissociation constants. The 1-20, but not the 1-16, peptide appears to adopt a helical conformation when bound to vesicles and cooperatively promotes vesicle fusion.