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Study of auto-organization in solution of hierarchical structures of peptide in presence of metallic nanoparticles

Grant number: 15/20446-9
Support Opportunities:Scholarships in Brazil - Doctorate (Direct)
Effective date (Start): August 01, 2017
Effective date (End): February 28, 2021
Field of knowledge:Physical Sciences and Mathematics - Chemistry - Physical-Chemistry
Principal Investigator:Wendel Andrade Alves
Grantee:Juliane Nogueira Batista Dias Pelin
Host Institution: Centro de Ciências Naturais e Humanas (CCNH). Universidade Federal do ABC (UFABC). Ministério da Educação (Brasil). Santo André , SP, Brazil
Associated scholarship(s):18/12535-0 - Self-organization of hierarchical structures of peptide in solution in presence of metallic nanoparticles, BE.EP.DD


The creation of peptides based on nanomaterials has stood out in recent decades due to its versatility and operational advantages. Besides have an easy and smooth synthetic routes, can be applied in various fields including regenerative medicine and cell culture, since they have numerous routes to its functionalization, which, consequently, can promote the formation of fibers, sheets, micelles and tubes. In this context, this project will investigate the nucleation process of the metal particles on substrates composed of mixed peptide sequences based mainly on L-phenylalanine (F), L-arginine (R) and L-cysteine (C) amino acids. Therefore, they will be studied by spectroscopic, microscopic and scatter techniques, the steps of nucleation, growth, and stabilization of the nanoparticles in amphiphilic peptides' colloidal solution. The selforganization process variables of these structures, such as constant critical aggregation and kinetic constants, will be determined as well as the physicochemical parameters of the medium: ionic strength, pH and solvent polarity. This is intended to establish an overview of inter and intramolecular interactions involved in the formation of hybrid structures containing peptides and metallic nanoparticles, which have potential application as matrices in asymmetric catalysis, since the peptide nanostructures settings formed can influence the stereoselectivity of these reactions. Results obtained using FFC sequence, prepared according to a solid phase Fmoc strategy, show that the peptide has different polymorphs in aqueous medium, depending on the concentration used. The Critical Aggregation Concentration (cac) found was 0.77 mmol L-1 and when in solution, FFC tends to self-organize in ²-sheet-like structures. In addition, it has been found that the incorporation of gold nanoparticles into the system may favor the process of inhibition or enhancement of amyloid fibers from the peptide aggregation process. Using sodium borohydride (NaBH4) as the reducing agent, a maximum absorption peak was obtained close to 520 nm, which suggests that the particles were dispersed, independent of the FFC concentration; however, by heating (60°C) the FFC and a gold salt solution mixture, were formed fibrillar materials decorated with gold nanoparticles. (AU)

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Scientific publications (8)
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
SOARES, BRUNA M.; SODRE, PEDRO T.; AGUILAR, ANDREA M.; GERBELLI, BARBARA B.; PELIN, JULIANE N. B. D.; ARGUELLO, KARINA B.; SILVA, EMERSON R.; DE FARIAS, MARCELO A.; PORTUGAL, RODRIGO V.; SCHMUCK, CARSTEN; et al. Structure optimization of lipopeptide assemblies for aldol reactions in an aqueous medium. Physical Chemistry Chemical Physics, v. 23, n. 18, p. 10953-10963, . (17/02317-2, 18/05888-3, 15/20446-9, 14/50867-3)
PELIN, JULIANE N. B. D.; EDWARDS-GAYLE, CHARLOTTE J. C.; CASTELLETTO, VALERIA; AGUILAR, ANDREA M.; ALVES, WENDEL A.; SEITSONEN, JANI; RUOKOLAINEN, JANNE; HAMLEY, IAN W.. Self-Assembly, Nematic Phase Formation, and Organocatalytic Behavior of a Proline-Functionalized Lipopeptide. ACS APPLIED MATERIALS & INTERFACES, v. 12, n. 12, p. 13671-13679, . (15/20446-9, 18/12535-0, 17/02317-2)
PELIN, JULIANE N. B. D.; GATTO, EMANUELA; VENANZI, MARIANO; CAVALIERI, FRANCESCA; OLIVEIRA, CRISTIANO L. P.; MARTINHO, HERCULANO; SILVA, EMERSON R.; AGUILAR, ANDREA M.; SOUZA, JULIANA S.; ALVES, WENDEL A.. Hybrid Conjugates Formed between Gold Nanoparticles and an Amyloidogenic Diphenylalanine-Cysteine Peptide. CHEMISTRYSELECT, v. 3, n. 24, p. 6756-6765, . (15/24018-1, 15/20446-9, 17/02317-2, 16/24409-3, 14/50867-3)
PELIN, JULIANE N. B. D.; EDWARDS-GAYLE, CHARLOTTE J. C.; AGUILAR, ANDREA M.; KAUR, AMANPREET; HAMLEY, IAN W.; ALVES, WENDEL A.. Polymorphism of asymmetric catalysts based on amphiphilic lipopeptides in solution. SOFT MATTER, v. 16, n. 19, p. 4615-4624, . (14/50867-3, 15/20446-9, 18/12535-0, 17/02317-2)
PELIN, JULIANE N. B. D.; GERBELLI, BARBARA B.; SOARES, BRUNA M.; AGUILAR, ANDREA M.; ALVES, WENDEL A.. Amyloidogenic model peptides as catalysts for stereoselective aldol reactions. CATALYSIS SCIENCE & TECHNOLOGY, v. 9, n. 16, p. 4304-4313, . (14/50867-3, 17/02317-2, 18/05888-3, 15/20446-9)
CASTELLETTO, VALERIA; EDWARDS-GAYLE, CHARLOTTE J. C.; HAMLEY, IAN W.; PELIN, JULIANE N. B. D.; ALVES, WENDEL A.; AGUILAR, ANDREA M.; SEITSONEN, JANI; RUOKOLAINEN, JANNE. Self-Assembly of a Catalytically Active Lipopeptide and Its Incorporation into Cubosomes. ACS APPLIED BIO MATERIALS, v. 2, n. 8, p. 9-pg., . (15/24018-1, 17/02317-2, 15/20446-9, 14/50867-3)
PELIN, JULIANE N. B. D.; EDWARDS-GAYLE, CHARLOTTE J. C.; MARTINHO, HERCULANO; GERBELLI, BARBARA B.; CASTELLETTO, VALERIA; HAMLEY, IAN W.; ALVES, WENDEL A.. Self-assembled gold nanoparticles and amphiphile peptides: a colorimetric probe for copper(ii) ion detection. DALTON TRANSACTIONS, v. 49, n. 45, p. 16226-16237, . (18/05888-3, 15/20446-9, 18/12535-0, 17/02317-2)
PELIN, JULIANE N. B. D.; GERBELLI, BARBARA B.; EDWARDS-GAYLE, CHARLOTTE J. C.; AGUILAR, ANDREA M.; CASTELLETTO, VALERIA; HAMLEY, IAN W.; ALVES, WENDEL A.. Amyloid Peptide Mixtures: Self-Assembly, Hydrogelation, Nematic Ordering, and Catalysts in Aldol Reactions. Langmuir, v. 36, n. 11, p. 2767-2774, . (14/50867-3, 17/02317-2, 18/05888-3, 18/12535-0, 15/20446-9)

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