A statistical investigation of amphiphilic properties of C-terminally anchored peptidases |
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Authors: | James?Wallace,Frederick?Harris,David?A.?Phoenix author-information" > author-information__contact u-icon-before" > mailto:daphoenix@uclan.ac.uk" title=" daphoenix@uclan.ac.uk" itemprop=" email" data-track=" click" data-track-action=" Email author" data-track-label=" " >Email author |
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Affiliation: | (1) Dean's Office, Faculty of Science, University of Central Lancashire, Preston, PR1 2HE, UK;(2) Department of Physics, Astronomy and Mathematics, University of Central Lancashire, Preston, PR1 2HE, UK;(3) Department of Forensic and Investigative Science, University of Central Lancashire, Preston, PR1 2HE, UK |
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Abstract: | A number of DD-peptidases have been reported to interact with the membrane via C-terminal amphiphilic α-helices, but experimental support for this rests with a few well-characterized cases. These show the C-terminal interactions of DD-carboxypeptidases to involve high levels of membrane penetration, DD-endopeptidases to involve membrane surface binding and class C penicillin-binding proteins to involve membrane binding with intermediate properties. Here, we have characterized C-terminal α-helices from each of these peptidase groups according to their amphiphilicity, as measured by mean <μH>, and the corresponding mean hydrophobicity, <H>. Regression and statistical analyses showed these properties to exhibit parallel negative linear relationships, which resulted from the spatial ordering of α-helix amino acid residues. Taken with the results of compositional and graphical analyses, our results suggest that the use of C-terminal α-helices may be a universal feature of the membrane anchoring for each of these groups of DD-peptidases. Moreover, to accommodate differences between these mechanisms, each group of C-terminal α-helices optimizes its structural amphiphilicity and hydrophobicity to fulfil its individual membrane-anchoring function. Our results also show that each anchor type analysed requires a similar overall balance between amphiphilicity for membrane interaction, which we propose is necessary to stabilize their initial membrane associations. In addition, we present a methodology for the prediction of C-terminal α-helical anchors from the classes of DD-peptidases analysed, based on a parallel linear model. |
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Keywords: | C-terminal amphiphilic α -helix DD-peptidase Membrane anchoring Penicillin-binding protein Regression with categorical predictors |
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