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Int. J. Mol. Sci. 2018, 19(8), 2447; https://doi.org/10.3390/ijms19082447

Effect of N- and C-Terminal Amino Acids on the Interfacial Binding Properties of Phospholipase D from Vibrio parahaemolyticus

1
School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China
2
Institut de Chimie et de Biochimie Moléculaires et Supramoléculaires (ICBMS), Université Lyon 1, Univ Lyon, UMR 5246 CNRS, Métabolisme, Enzymes et Mécanismes Moléculaires (MEM2), Bât Raulin, 43 Bd du 11 Novembre 1918, CEDEX, F-69622 Villeurbanne, France
3
School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China
*
Author to whom correspondence should be addressed.
Received: 26 July 2018 / Revised: 13 August 2018 / Accepted: 16 August 2018 / Published: 19 August 2018
(This article belongs to the Special Issue Microbial Enzymes)
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Abstract

The effects of N-terminal (1–34 amino acids) and C-terminal (434–487 amino acids) amino acid sequences on the interfacial binding properties of Phospholipase D from Vibrio parahaemolyticus (VpPLD) were characterized by using monomolecular film technology. Online tools allowed the prediction of the secondary structure of the target N- and C-terminal VpPLD sequences. Various truncated forms of VpPLD with different N- or C-terminal deletions were designed, based on their secondary structure, and their membrane binding properties were examined. The analysis of the maximum insertion pressure (MIP) and synergy factor “a” indicated that the loop structure (1–25 amino acids) in the N-terminal segment of VpPLD had a positive effect on the binding of VpPLD to phospholipid monolayers, especially to 1,2-dimyristoyl-sn-glycero-3-phosphoserine and 1,2-dimyristoyl-sn-glycero-3-phosphocholine. The deletion affecting the N-terminus loop structure caused a significant decrease of the MIP and synergy factor a of the protein for these phospholipid monolayers. Conversely, the deletion of the helix structure (26–34 amino acids) basically had no influence on the binding of VpPLD to phospholipid monolayers. The deletion of the C-terminal amino acids 434–487 did not significantly change the binding selectivity of VpPLD for the various phospholipid monolayer tested here. However, a significant increase of the MIP value for all the phospholipid monolayers strongly indicated that the three-strand segment (434–469 amino acids) had a great negative effect on the interfacial binding to these phospholipid monolayers. The deletion of this peptide caused a significantly greater insertion of the protein into the phospholipid monolayers examined. The present study provides detailed information on the effect of the N- and C-terminal segments of VpPLD on the interfacial binding properties of the enzyme and improves our understanding of the interactions between this enzyme and cell membranes. View Full-Text
Keywords: Phospholipase D; Vibrio parahaemolyticus; interfacial properties; monomolecular film; binding parameters Phospholipase D; Vibrio parahaemolyticus; interfacial properties; monomolecular film; binding parameters
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Wang, F.; Wei, R.; Abousalham, A.; Chen, W.; Yang, B.; Wang, Y. Effect of N- and C-Terminal Amino Acids on the Interfacial Binding Properties of Phospholipase D from Vibrio parahaemolyticus. Int. J. Mol. Sci. 2018, 19, 2447.

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