Self-Assembly of Arg鈥揚he Nanostructures via the Solid鈥揤apor Phase Method

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• 作者：Michelle S. Liberato ; Sergio Kogikoski ; Jr. ; Emerson R. Silva ; Mauricio D. Coutinho-Neto ; Luis P. B. Scott ; Ricardo H. Silva ; Vani X. Oliveira ; Jr. ; R么mulo A. Ando ; Wendel A. Alves
• 刊名：The Journal of Physical Chemistry B
• 出版年：2013
• 出版时间：January 24, 2013
• 年：2013
• 卷：117
• 期：3
• 页码：733-740
• 全文大小：536K
• 年卷期：v.117,no.3(January 24, 2013)
• ISSN：1520-5207

文摘

We report for the first time on the self-assembly of nanostructures composed exclusively of alternating positively charged and hydrophobic amino acids. A novel arginine/phenylalanine octapeptide, RF8, was synthesized. Because the low hydrophobicity of this sequence makes its spontaneous ordering through solution-based methods difficult, a recently proposed solid鈥搗apor approach was used to obtain nanometric architectures on ITO/PET substrates. The formation of the nanostructures was investigated under different preparation conditions, specifically, under different gas-phase solvents (aniline, water, and dichloromethane), different peptide concentrations in the precursor solution, and different incubation times. The stability of the assemblies was experimentally studied by electron microscopy and thermogravimetric analysis coupled with mass spectrometry. The secondary structure was assessed by infrared and Raman spectroscopy, and the arrays were found to assume an antiparallel 尾-sheet conformation. FEG-SEM images clearly reveal the appearance of fibrillar structures that form extensive homogeneously distributed networks. A close relationship between the morphology and preparation parameters was found, and a concentration-triggered mechanism was suggested. Molecular dynamics simulations were performed to address the thermal stability and nature of intermolecular interactions of the putative assembly structure. Results obtained when water is considered as solvent shows that a stable lamellar structure is formed containing a thin layer of water in between the RF8 peptides that is stabilized by H-bonding.