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Structural organization and bioactivity in peptide and nucleotide self-assemblies

Abstract

Nucleic acids and peptides occupy a privileged position in the spectrum of materials intended for the fabrication of bionanostructures. These molecular species exhibit high physicochemical versatility along with intrinsic biocompatibility. Inspired by these unique properties, in this project we aim to formulate nanostructured materials based on self-assembling bioactive peptides and nucleotides. A range of advanced techniques including infrared nano spectroscopy, time-resolved small-angle X-ray scattering, atomic force microscopy in liquid medium and coherent anti-Stokes Raman scattering microscopy will be used to provide a detailed portrait of these nanoparticles across the mesoscale, from their secondary structure to interaction with cell membranes at micrometer range. Our focus will be on three major classes of bioactive peptides: cell penetrating peptides, extracellular matrix constituents (collagen- and elastin-like sequences) and anti-inflammatory peptides. The nucleotide building blocks will be monophosphates based on the purine nucleobases adenine and guanine (AMP and GMP). The capabilities of these scaffolds to encapsulate model drugs will be investigated.In addition to deep structural characterization, we aim to test bioactivity to determine if functions exhibited by molecular blocks are preserved or even enhanced upon organization into superstructures. Based on both structural and bioactivity data we aim to stablish structure-activity relationships and contribute for optimizing the formulation of biomedical materials based on these bioactive molecules. (AU)

Scientific publications
(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)
GERBELLI, BARBARA B.; OLIVEIRA, CRISTIANO L. P.; SILVA, EMERSON R.; HAMLEY, IAN W.; ALVES, WENDEL A. Amyloid Formation by Short Peptides in the Presence of Dipalmitoylphosphatidylcholine Membranes. Langmuir, v. 36, n. 48, p. 14793-14801, DEC 8 2020. Web of Science Citations: 0.

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