Self-Assembly of Arg-Phe Nanostructures via the Solid-Vapor Phase Method

Autor(es)

Liberato, Michelle S. ^[1] ; Kogikoski, Jr., Sergio ^[1] ; Silva, Emerson R. ^[1] ; Coutinho-Neto, Mauricio D. ^[1] ; Scott, Luis P. B. ^[1] ; Silva, Ricardo H. ^[1] ; Oliveira, Jr., Vani X. ^[1] ; Ando, Romulo A. ^[2] ; Alves, Wendel A. ^[1]

Afiliação do(s) autor(es)

^[1] Univ Fed ABC, Ctr Ciencias Nat & Humanas, BR-09210170 Santo Andre, SP - Brazil

^[2] Univ Sao Paulo, Inst Quim, BR-05513970 Sao Paulo - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Journal of Physical Chemistry B; v. 117, n. 3, p. 733-740, JAN 24 2013.
• Citações Web of Science: 14

Resumo

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-vapor 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 beta-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. (AU)

• Processo FAPESP: 12/01933-8 - Matrizes biomiméticas obtidas por eletrofiação: possível aplicação na detecção de NO
• Beneficiário: Sergio Kogikoski Junior
• Modalidade de apoio: Bolsas no Brasil - Doutorado Direto
• Processo FAPESP: 10/09306-7 - Desenvolvimento de metodologia para simular docking flexível com alterações específicas na estrutura primária e as aplicações dessa metodologia para estudar interação proteína-proteína, proteína-ligante e resistência de patógenos a drogas
• Beneficiário: Ana Lígia Barbour Scott
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 05/60596-8 - Espécies complexas com potencial aplicação em bioinorgânica, catálise, farmacologia e química ambiental: concepção, preparação, caracterização e reatividade
• Beneficiário: Ana Maria da Costa Ferreira
• Modalidade de apoio: Auxílio à Pesquisa - Temático
• Processo FAPESP: 09/12153-0 - Síntese e Caracterização de Nanoestruturas Peptídicas: Estudos Espectroscópicos e Aplicações
• Beneficiário: Michelle da Silva Liberato
• Modalidade de apoio: Bolsas no Brasil - Mestrado
• Processo FAPESP: 08/53576-9 - Síntese, caracterização e estudo das propriedades eletrônicas dos nanotubos de peptídeos e óxido de titânio
• Beneficiário: Wendel Andrade Alves
• Modalidade de apoio: Auxílio à Pesquisa - Jovens Pesquisadores
• Processo FAPESP: 08/57805-2 - Instituto de Bioanalítica
• Beneficiário: Lauro Tatsuo Kubota
• Modalidade de apoio: Auxílio à Pesquisa - Temático