Morphology and structural properties of pH-responsive amphiphilic peptides.
Morphology and structural properties of pH-responsive amphiphilic peptides.
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pH 响应型两亲肽的形态和结构特性。
DOI:
10.1166/jnn.2010.2996
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发表时间:
2010
影响因子:
--
通讯作者:
Sun,XiuzhiSusan
中科院分区:
文献类型:
--
作者:
Shera,JeanneN;Takahashi,Daisuke;Herrera,AlvaroI;Prakash,Om;Sun,XiuzhiSusan
Protein nanomaterials at the peptide level have shown great potential for medical applications. Peptides change their morphological conformation because of changes in self-assembly properties when they are exposed to changes in solvent composition or pH. Two 15-residue peptide sequences, KhK (KKKFLIVIGSIIKKK) and Alternating Kh (KFLKKIVKIGKKSII), were designed for the purpose of determining the role of peptide sequence on solution morphology and conformation. KhK solutions exhibited a random coil to helical transition when solvent conditions were changed from water to a trifluorethanol/water solution at acidic pH. Alternating Kh solutions, however, demonstrated primarily random coil character under similar solvent and pH conditions as determined by circular dichroism spectroscopy and 2D-1H–1H nuclear magnetic resonance spectroscopy. At basic pH, circular dichroism spectroscopy and nuclear magnetic resonance spectroscopy analysis demonstrated that random coil character increased at basic pH for KhK, whereas Alternating Kh exhibited an increase in -sheet character. Further analysis by transmission electron microscopy showed marked differences in the peptide solution morphology. Peptide particle aggregation and fiber formation were significantly affected by solvent composition and pH values for both peptide sequences.