The interaction of proteins with silica surfaces. Part I: Ab initio modeling

• Published in: Computational and theoretical chemistry Vol. 1117; pp. 100 - 107
• Main Authors: Trachta, Michal, Bludský, Ota, Rubeš, Miroslav
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.10.2017
• Subjects: 2D zeolites; Amino acids; DFT; Dispersion; Side chains; Silica; Amino acids; 2D zeolites; DFT; Silica; Side chains; Dispersion
• ISSN: 2210-271X
• DOI: 10.1016/j.comptc.2017.07.019

[Display omitted] •Side-chain silica interactions are not described accurately with DC-DFT methods.•Very different behavior is observed on surfaces with/without silanol groups.•New development is required to reach chemical accuracy for FF parameterization.•Two different methodologies were proposed and provided consistent results. Recently synthesized 2D zeolites with well-defined external surfaces have been used as model systems for the adsorption of proteins on silica materials. In this work the interaction of 19 proteinogenic amino-acid side chains in the Cβ representation and the Ace-NMe backbone model with the 2D-UTL and 2D-MWW zeolites has been investigated. The performance of different DC-DFT methods has been compared against the MP2/CBS and CCSD(T)/CBS levels of theory for cluster models of α-quartz and 2D-UTL. The obtained statistics clearly indicate that none of the common DC-DFT methods is capable of describing the side-chain interaction with silica surfaces within chemical accuracy (∼1kcal/mol). Two different approaches have been employed to improve the accuracy: (i) the re-parameterization of the pair-wise dispersion term as proposed by Grimme 2006 and (ii) the correction scheme based on an error analysis of the vdW-DF2 functional. Both methods provide consistent and highly accurate results for external silica surfaces with and without silanol groups.