期刊
LANGMUIR
卷 25, 期 16, 页码 8849-8853出版社
AMER CHEMICAL SOC
DOI: 10.1021/la901342r
关键词
-
资金
- National Basic Research Program of China [2009CB930100]
- CAS Key Laboratory of Nano Bioeffect and Biosafety
Molecular structures of polypeptide molecules (DELERIRELEARIK) adsorbed at liquid-solid interfaces of graphite have been studied using scanning tunneling microscopy (STM). The polypeptide is originally stable with all alpha-helical conformation in solution and in its crystal states. STM observations reveal that the adsorbed polypeptides form homogeneous beta-sheet-like assemblies on the graphite surface. The separation (4.7 +/- 0.1 angstrom) between two neighboring polypeptides and the full lengths of the polypeptides determined front STM images suggest distinctively different molecular conformations from the alpha-helical structure. The N 1s peak in the X-ray photoelectron spectroscopy (XPS) spectrum confirmed the presence of polypeptides on the graphite surface. In addition, the circular dichroism (CD) results provide supporting evidence that the polypeptides would undergo a structural transformation to beta-sheet secondary structure upon the addition of graphite particles to the peptide solution. Such conformational rearrangements upon adsorption oil a hydrophobic Surface could benefit the studies oil protein-surface interactions.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据