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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Adsorption of lysozyme into a charged confining pore

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Author(s):
Caetano, Daniel L. Z. [1, 2] ; Metzler, Ralf [3] ; Cherstvy, Andrey G. [4, 3] ; de Carvalho, Sidney J. [5]
Total Authors: 4
Affiliation:
[1] Univ Estadual Campinas, Inst Chem, State Univ Campinas, Campinas, SP - Brazil
[2] Univ Estadual Campinas, Ctr Computat Engn & Sci, State Univ Campinas, Campinas, SP - Brazil
[3] Univ Potsdam, Inst Phys & Astron, D-14476 Potsdam - Germany
[4] Humboldt Univ, Inst Phys, D-12489 Berlin - Germany
[5] Sao Paulo State Univ, Inst Biosci Humanities & Exact Sci, Dept Phys, UNESP, Sao Jose Do Rio Preto - Brazil
Total Affiliations: 5
Document type: Journal article
Source: Physical Chemistry Chemical Physics; v. 23, n. 48 NOV 2021.
Web of Science Citations: 0
Abstract

Several applications arise from the confinement of proteins on surfaces because their stability and biological activity are enhanced. It is also known that the way in which a protein adsorbs on the surface is important for its biological function since its active sites should not be obstructed. In this study, the adsorption properties of hen egg-white lysozyme, HEWL, into a negatively charged silica pore is examined by employing a coarse-grained model and constant-pH Monte Carlo simulations. The role of electrostatic interactions is taken into account via including the Debye-Huckel potentials into the C alpha structure-based model. We evaluate the effects of pH, salt concentration, and pore radius on the protein preferential orientation and spatial distribution of its residues regarding the pore surface. By mapping the residues that stay closer to the pore surface, we find that the increase of pH leads to orientational changes of the adsorbed protein when the solution pH gets closer to the HEWL isoelectric point. Under these conditions, the pK(a) shift of these important residues caused by the adsorption into the charged confining surface results in a HEWL charge distribution that stabilizes the adsorption in the observed protein orientation. We compare our observations to the results of the pK(a) shift for HEWL available in the literature and to some experimental data. (AU)

FAPESP's process: 13/08293-7 - CCES - Center for Computational Engineering and Sciences
Grantee:Munir Salomao Skaf
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 18/01841-2 - Computational Simulation Studies on the Interaction Between Polyelectrolytes and Macromolecules
Grantee:Sidney Jurado de Carvalho
Support Opportunities: Regular Research Grants
FAPESP's process: 19/19662-0 - Mesoscopic architecture of lignocellulosic fibers
Grantee:Daniel Lucas Zago Caetano
Support Opportunities: Scholarships in Brazil - Post-Doctoral