期刊
LANGMUIR
卷 29, 期 22, 页码 6665-6672出版社
AMER CHEMICAL SOC
DOI: 10.1021/la401025r
关键词
-
资金
- EPSRC [EP/G026203/1, G067538/1]
- Engineering and Physical Sciences Research Council [EP/G026203/1, EP/G067538/1] Funding Source: researchfish
- EPSRC [EP/G067538/1, EP/G026203/1] Funding Source: UKRI
The enzymatic cleavage of a peptide amphiphile (PA) is investigated. The self-assembly of the cleaved products is distinct from that of the PA substrate. The PA C-16-KKFFVLK is cleaved by alpha-chymotrypsin at two sites leading to products C-16-KKF with FVLK and C-16-KKFF with VLK. The PA C-16-KKFFVLK forms nanotubes and helical ribbons at room temperature. Both PAs C-16-KKF and C-16-KKFF corresponding to cleavage products instead self-assemble into 5-6 nm diameter spherical micelles, while peptides FVLK and VLK do not adopt well-defined aggregate structures. The secondary structures of the PAs and peptides are examined by FTIR and circular dichroism spectroscopy and X-ray diffraction. Only C-16-KKFFVLK shows substantial beta-sheet secondary structure, consistent with its self-assembly into extended aggregates, based on PA layers containing hydrogen-bonded peptide headgroups. This PA also exhibits a thermoreversible transition to twisted tapes on heating.
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