Tuning self-assembled nanostructures through enzymatic degradation of a peptide amphiphile.
Tuning self-assembled nanostructures through enzymatic degradation of a peptide amphiphile.
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DOI：
10.1021/la401025r
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发表时间：
2013-06-04
期刊：
影响因子：
--
通讯作者：
Ruokolainen J
中科院分区：
文献类型：
--
作者：
Dehsorkhi A;Hamley IW;Seitsonen J;Ruokolainen J
研究了肽两亲物（PA）的酶促裂解。裂解产物的自组装不同于PA底物的自组装。PA C16-KKFFVLK在两个位点被α-胰凝乳蛋白酶裂解，产生产物C16-KKF与FVLK和C16-KKFF与VLK。PA C16-KKFFVLK在室温下形成纳米管和螺旋带。对应于裂解产物的PA C16-KKF和C16-KKFF两者反而自组装成5-6 nm直径的球形胶束，而肽FVLK和VLK不采用明确定义的聚集体结构。通过红外光谱、圆二色谱和X射线衍射对产物的二级结构进行了表征。只有C16-KKFFVLK显示出大量的β-折叠二级结构，这与其自组装成延伸的聚集体一致，基于含有氢键键合的肽头基的PA层。该PA还表现出在加热时向扭曲带的热可逆转变。
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 C16-KKFFVLK is cleaved by α-chymotrypsin at two sites leading to products C16-KKF with FVLK and C16-KKFF with VLK. The PA C16-KKFFVLK forms nanotubes and helical ribbons at room temperature. Both PAs C16-KKF and C16-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 C16-KKFFVLK shows substantial β-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.
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影响因子：
2.9
作者：
HARIS, PI;CHAPMAN, D
通讯作者：
CHAPMAN, D
用于制作功能生物学材料的肽自组装。
DOI：
10.1016/j.cossms.2011.08.001
发表时间：
2011-12
影响因子：
11
作者：
Matson, John B.;Zha, R. Helen;Stupp, Samuel I.
通讯作者：
Stupp, Samuel I.
影响因子：
38.3
作者：
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通讯作者：
Discher, Dennis E.
影响因子：
2.9
作者：
Krysmann, Marta J.;Castelletto, Valeria;Pochan, Darrin J.
通讯作者：
Pochan, Darrin J.
影响因子：
3.9
作者：
Lahari, Challa;Jasti, Lakshmi S.;Ponrathnam, Surendra
通讯作者：
Ponrathnam, Surendra