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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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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]
Total Authors: 9
[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
Total Affiliations: 2
Document type: Journal article
Source: Journal of Physical Chemistry B; v. 117, n. 3, p. 733-740, JAN 24 2013.
Web of Science Citations: 14

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)

FAPESP's process: 09/12153-0 - Synthesis and Characterization of Peptide Nanostructures: Spectroscopic Studies and Applications
Grantee:Michelle da Silva Liberato
Support type: Scholarships in Brazil - Master
FAPESP's process: 10/09306-7 - Developing a methodology to simulate flexible complete docking and specific mutation in the primary structure and its applications to study interaction protein-protein, protein-ligand and resistance of pathogenesis and drugs
Grantee:Ana Ligia Scott
Support type: Regular Research Grants
FAPESP's process: 12/01933-8 - Biomimetic electrospun matrixes: possible application in NO detection
Grantee:Sergio Kogikoski Junior
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 05/60596-8 - Complex species with potential for application in bio-organics, catalysis, pharmacology and environmental chemistry: conception, preparation, characterization and reactivity
Grantee:Ana Maria da Costa Ferreira
Support type: Research Projects - Thematic Grants
FAPESP's process: 08/57805-2 - Institute of Bioanalytics
Grantee:Lauro Tatsuo Kubota
Support type: Research Projects - Thematic Grants