Please use this identifier to cite or link to this item: http://repositorio.ufla.br/jspui/handle/1/40232
Title: Thermodynamics of multi-walled carbon nanotube biofunctionalization using nisin: the effect of peptide structure
Keywords: Nisin
Adsorption
Carbon nanotube
Thermodynamics
Biocomplex
Issue Date: Oct-2019
Publisher: Elsevier
Citation: FERREIRA, G. M. D. et al. Thermodynamics of multi-walled carbon nanotube biofunctionalization using nisin: the effect of peptide structure. Colloids and Surfaces A: Physicochemical and Engineering Aspects, [S.l.], v. 578, Oct. 2019.
Abstract: A detailed adsorption thermodynamic study of two nisin variants (nisA and nisZ) on multi-walled carbon nanotubes (MWCNT) was conducted, and the antimicrobial properties of biofunctionalized MWCNT were evaluated. The MWCNT adsorption capacity for peptides () increased with pH increase, with greater values for nisZ ( up to 250 mg g−1) than for nisA ( up to 180 mg g−1) for all studied conditions. Zeta potential measurements (ζ) showed that the electrostatic repulsion between the MWCNT-peptide complexes determined the dispersion features that were stable at pH 2.0 and 3.0, with ζ reaching 45.0 mV at the lowest pH. Despite the similar ζ values for both peptides, slightly greater stabilization of MWCNT dispersions was exhibited in presence of nisZ at pH 3. At pH 4 and 5, peptide adsorption was not able to promote MWCNT dispersibility. Isothermal titration calorimetry revealed that the adsorption process was driven by enthalpy for both peptides, as the adsorption enthalpy changes () were less negative than −99.7 kJ mol−1. Despite the large dependence of on the pH and values, indicating the important role of electrostatic interactions on the adsorption process, a change in only one amino acid residue in the nisin structure promoted intense changes in the adsorption thermodynamic parameters. We have suggested that the more hydrophobic character of nisZ at the lower pH values caused this peptide to interact with the MWCNT surface through its two domains. Interesting, the antimicrobial properties of both peptides were not damaged, and the functionalized MWCNT showed antibacterial activity against the indicator micro-organism Lactococcus lactis in the agar diffusion and solution assays.
URI: https://www.sciencedirect.com/science/article/abs/pii/S0927775719305941
http://repositorio.ufla.br/jspui/handle/1/40232
Appears in Collections:DQI - Artigos publicados em periódicos

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