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Hydrolysis of Chemically Distinct Sites of Human Serum Albumin by Polyoxometalate: A Hybrid QM/MM (ONIOM) Study
Univ Miami, Dept Chem, Coral Gables, FL 33146 USA.
Univ Miami, Dept Chem, Coral Gables, FL 33146 USA.
Univ Miami, Dept Chem, Coral Gables, FL 33146 USA.
Univ Miami, Dept Chem, Coral Gables, FL 33146 USA.
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2019 (English)In: Journal of Computational Chemistry, ISSN 0192-8651, E-ISSN 1096-987X, Vol. 40, no 1, p. 51-61Article in journal (Refereed) Published
Abstract [en]

In this study, mechanisms of hydrolysis of all four chemically diverse cleavage sites of human serum albumin (HSA) by [Zr(OH) (PW11O39)](4-)(ZrK) have been investigated using the hybrid two-layer QM/MM (ONIOM) method. These reactions have been proposed to occur through the following two mechanisms: internal attack (IA) and water assisted (WA). In both mechanisms, the cleavage of the peptide bond in the Cys392-Glu393 site of HSA is predicted to occur in the rate-limiting step of the mechanism. With the barrier of 27.5 kcal/mol for the hydrolysis of this site, the IA mechanism is found to be energetically more favorable than the WA mechanism (barrier = 31.6 kcal/mol). The energetics for the IA mechanism are in line with the experimentally measured values for the cleavage of a wide range of dipeptides. These calculations also suggest an energetic preference (Cys392-Glu393, Ala257-Asp258, Lys313-Asp314, and Arg114-Leu115) for the hydrolysis of all four sites of HSA. (C) 2018 Wiley Periodicals, Inc.

Place, publisher, year, edition, pages
2019. Vol. 40, no 1, p. 51-61
Keywords [en]
polyoxometalates, human serum albumin, peptide hydrolysis, reaction mechanism, QM/MM (ONIOM) method
National Category
Theoretical Chemistry Physical Chemistry
Identifiers
URN: urn:nbn:se:uu:diva-372750DOI: 10.1002/jcc.25528ISI: 000452421800005PubMedID: 30238478OAI: oai:DiVA.org:uu-372750DiVA, id: diva2:1278974
Available from: 2019-01-15 Created: 2019-01-15 Last updated: 2019-01-15Bibliographically approved

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Lundberg, Marcus

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