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Title: Thermodynamics of multi-walled carbon nanotube biofunctionalization using nisin : the effect of peptide structure.
Authors: Ferreira, Guilherme Max Dias
Ferreira, Gabriel Max Dias
Almeida, Germanna Wilk Reis de
Soares, Nilda de Fatima Ferreira
Pires, Ana Clarissa dos Santos
Silva, Luis Henrique Mendes da
Keywords: Adsorption
Issue Date: 2019
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, v. 578, n. 123611, out. 2019. Disponível em: <>. Acesso em: 10 fev. 2020.
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.
ISSN: 0927-7757
Appears in Collections:DEQUI - Artigos publicados em periódicos

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