Nanostructures from protected L/L and D/L amino acid containing dipeptides
Nanostructures from protected L/L and D/L amino acid containing dipeptides
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DOI：
10.1002/pep2.24176
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发表时间：
2020-06-17
期刊：
影响因子：
2.4
通讯作者：
Mandal, Bhubaneswar
中科院分区：
文献类型：
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作者：
Giri, Rajat Subhra;Pal, Saikat;Mandal, Bhubaneswar
研究了N-和C-保护的交替L/L和D/L氨基酸的二肽Boc-L-Val-L-Ile-OMe（1）、Boc-D-Val-L-Ile-OMe（2）、Boc-L-IleL-Val-OMe（3）和Boc-L-Ile-D-Val-OMe（4）的自组装。场发射扫描电子显微镜（FESEM）和原子力显微镜（AFM）图像表明，1和3自缔合形成高度有序的直网状微棒，2和4自组装形成六边形中空微管状结构.为了理解这种差异行为的物理基础，我们进行了X射线衍射图案分析。单晶X射线衍射（SC-XRD）研究表明，1和2自组装形成略有不同的螺旋状结构。2的高次缔合呈现中空的六角管状超结构。纳米结构的热稳定性也根据二肽的手性组成而变化。实验结果与计算研究相吻合。所获得的结果可能有助于纳米生物技术以及材料科学。
The self-assembly of N- and C-protected alternating L/L and D/L amino acids containing dipeptides, Boc-L-Val-L-Ile-OMe (1), Boc-D-Val-L-Ile-OMe (2), Boc-L-IleL-Val-OMe (3), and Boc-L-Ile-D-Val-OMe (4) has been investigated. Field emission scanning electron microscopy (FESEM) and atomic force microscopy (AFM) images indicated that 1 and 3 self-associated to form highly organized straight net microrods, whereas 2 and 4 self-assembled to form hexagonal hollow microtube-like architecture in the acetonitrile-water medium. To understand the physical basis of such differential behavior, we performed X-ray diffraction pattern analyses. The single-crystal X-ray diffraction (SC-XRD) study revealed that 1 and 2 self-assembled to form slightly different helix-like architectures. The higher-order association of 2 exhibited a hollow hexagonal tube-like superstructure. The thermal stability of the nanostructures also varied based on the chiroptical composition of the dipeptides. Experimental findings were corroborated well with computational studies. The obtained results may be helpful in nano-biotechnology as well as in material science.