Adsorption of flexible proteins in the 'wrong side' of the isoelectric point: Casein macropeptide as a model system.

Autor: Blanco PM; Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Hlavova 8, 128 00 Prague 2, Czech Republic; Department of Material Science and Physical Chemistry & Institute of Theoretical and Computational Chemistry (IQTC), University of Barcelona, C/ Martí i Franquès, 1, 08028 Barcelona, Catalonia, Spain., Achetoni MM; Universidad Tecnología Nacional & Grupo Bionanotecnología y Sistemas Complejos. (UTN-CONICET), Facultad Regional San Rafael, Av. General Urquiza 314C.P.:5600, San Rafael, Mendoza, Argentina., Garcés JL; Department of Chemistry, University of Lleida, Av. Alcalde Rovira Roure 191, E-25198 Lleida, Catalonia, Spain., Madurga S; Department of Material Science and Physical Chemistry & Institute of Theoretical and Computational Chemistry (IQTC), University of Barcelona, C/ Martí i Franquès, 1, 08028 Barcelona, Catalonia, Spain., Mas F; Department of Material Science and Physical Chemistry & Institute of Theoretical and Computational Chemistry (IQTC), University of Barcelona, C/ Martí i Franquès, 1, 08028 Barcelona, Catalonia, Spain., Baieli MF; Universidad de Buenos Aires & Instituto de Nanobiotecnología (UBA-CONICET), Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina., Narambuena CF; Universidad Tecnología Nacional & Grupo Bionanotecnología y Sistemas Complejos. (UTN-CONICET), Facultad Regional San Rafael, Av. General Urquiza 314C.P.:5600, San Rafael, Mendoza, Argentina. Electronic address: claudionarambuena@gmail.com.
Jazyk: angličtina
Zdroj: Colloids and surfaces. B, Biointerfaces [Colloids Surf B Biointerfaces] 2022 Sep; Vol. 217, pp. 112617. Date of Electronic Publication: 2022 Jun 10.
DOI: 10.1016/j.colsurfb.2022.112617
Abstrakt: We analyze the conditions of the adsorption of a flexible peptide onto a charged substrate in the 'wrong side' of the isoelectric point (WSIP), i.e. when surface and peptide charges have the same sign. As a model system, we focus on the casein macropeptide (CMP), both in the aglycosylated (aCMP) and fully glycosydated (gCMP) forms. We model the substrate as a uniformly charged plane while CMP is treated as a bead-and-spring model including electrostatic interactions, excluded volume effects and acid/base equilibria. Adsorption coverage, aminoacid charges and concentration profiles are computed by means of Monte Carlo simulations at fixed pH and salt concentration. We conclude that for different reasons the CMP can be adsorbed to both positively and negatively charged surfaces in the WSIP. For negatively charged surfaces, WSIP adsorption is due to the patchy distribution of charges: the peptide is attached to the surface by the positively charged end of the chain, while the repulsion of the surface for the negatively charged tail is screened by the small ions of the added salt. This effect increases with salt concentration. Conversely, a positively charged substrate induces strong charge regulation of the peptide: the acidic groups are deprotonated, and the peptide becomes negatively charged. This effect is stronger at low salt concentrations and it is more intense for gCMP than for aCMP, due to the presence of the additional sialic groups in gCMP.
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Databáze: MEDLINE
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