Skip to content

Glucose interactions with a model peptide

Research output: Contribution to journalArticle

Standard

Glucose interactions with a model peptide. / Mason, PE; Lerbret, A; Saboungi, M-L; Neilson, GW; Dempsey, CE; Brady, JW.

In: Proteins: Structure, Function, and Bioinformatics, Vol. 79 (7), 07.2011, p. 2224 - 2232.

Research output: Contribution to journalArticle

Harvard

Mason, PE, Lerbret, A, Saboungi, M-L, Neilson, GW, Dempsey, CE & Brady, JW 2011, 'Glucose interactions with a model peptide', Proteins: Structure, Function, and Bioinformatics, vol. 79 (7), pp. 2224 - 2232. https://doi.org/10.1002/prot.23047

APA

Mason, PE., Lerbret, A., Saboungi, M-L., Neilson, GW., Dempsey, CE., & Brady, JW. (2011). Glucose interactions with a model peptide. Proteins: Structure, Function, and Bioinformatics, 79 (7), 2224 - 2232. https://doi.org/10.1002/prot.23047

Vancouver

Mason PE, Lerbret A, Saboungi M-L, Neilson GW, Dempsey CE, Brady JW. Glucose interactions with a model peptide. Proteins: Structure, Function, and Bioinformatics. 2011 Jul;79 (7):2224 - 2232. https://doi.org/10.1002/prot.23047

Author

Mason, PE ; Lerbret, A ; Saboungi, M-L ; Neilson, GW ; Dempsey, CE ; Brady, JW. / Glucose interactions with a model peptide. In: Proteins: Structure, Function, and Bioinformatics. 2011 ; Vol. 79 (7). pp. 2224 - 2232.

Bibtex

@article{fb3fb5547d24476397f29e502f3035a3,
title = "Glucose interactions with a model peptide",
abstract = "Molecular dynamics simulations have been conducted of the helical polypeptide melittin, in concentrated aqueous solutions of the alpha and beta anomers of D-glucopyranose. Glucose is an osmolyte, and it is expected to be preferentially excluded from the surfaces of proteins. This was indeed found to be the case in the simulations. The results indicate that the observed exclusion may have a contribution from an under-representation of hydrogen bonding interactions between glucose groups and exposed side chains, compared to water. However, glucose was found to bind quite specifically to melittin by stacking its hydrophobic face, consisting of aliphatic protons, against the flat hydrophobic face of the indole group of the tryptophan-19 side chain. Although the binding site for this interaction is localized, the binding is weak for both anomers, with a binding free energy estimated as only ∼0.5 kcal/mol (i.e. near kBT). The face of the sugar stacked against the Trp indole ring is different for the two anomers of glucose, due to the disruption of the H1-H3-H5 hydrophobic triad of the beta anomer by the axial C1 hydroxyl group in the alpha anomer. The measurable affinity of the sugar for the Trp side chain is consistent with the very frequent occurrence of this group in the binding sites of proteins that complex with sugars. Proteins 2011; {\circledC} 2011 Wiley-Liss, Inc.",
author = "PE Mason and A Lerbret and M-L Saboungi and GW Neilson and CE Dempsey and JW Brady",
year = "2011",
month = "7",
doi = "10.1002/prot.23047",
language = "English",
volume = "79 (7)",
pages = "2224 -- 2232",
journal = "Proteins: Structure, Function, and Bioinformatics",
issn = "0887-3585",
publisher = "Wiley-Liss Inc.",

}

RIS - suitable for import to EndNote

TY - JOUR

T1 - Glucose interactions with a model peptide

AU - Mason, PE

AU - Lerbret, A

AU - Saboungi, M-L

AU - Neilson, GW

AU - Dempsey, CE

AU - Brady, JW

PY - 2011/7

Y1 - 2011/7

N2 - Molecular dynamics simulations have been conducted of the helical polypeptide melittin, in concentrated aqueous solutions of the alpha and beta anomers of D-glucopyranose. Glucose is an osmolyte, and it is expected to be preferentially excluded from the surfaces of proteins. This was indeed found to be the case in the simulations. The results indicate that the observed exclusion may have a contribution from an under-representation of hydrogen bonding interactions between glucose groups and exposed side chains, compared to water. However, glucose was found to bind quite specifically to melittin by stacking its hydrophobic face, consisting of aliphatic protons, against the flat hydrophobic face of the indole group of the tryptophan-19 side chain. Although the binding site for this interaction is localized, the binding is weak for both anomers, with a binding free energy estimated as only ∼0.5 kcal/mol (i.e. near kBT). The face of the sugar stacked against the Trp indole ring is different for the two anomers of glucose, due to the disruption of the H1-H3-H5 hydrophobic triad of the beta anomer by the axial C1 hydroxyl group in the alpha anomer. The measurable affinity of the sugar for the Trp side chain is consistent with the very frequent occurrence of this group in the binding sites of proteins that complex with sugars. Proteins 2011; © 2011 Wiley-Liss, Inc.

AB - Molecular dynamics simulations have been conducted of the helical polypeptide melittin, in concentrated aqueous solutions of the alpha and beta anomers of D-glucopyranose. Glucose is an osmolyte, and it is expected to be preferentially excluded from the surfaces of proteins. This was indeed found to be the case in the simulations. The results indicate that the observed exclusion may have a contribution from an under-representation of hydrogen bonding interactions between glucose groups and exposed side chains, compared to water. However, glucose was found to bind quite specifically to melittin by stacking its hydrophobic face, consisting of aliphatic protons, against the flat hydrophobic face of the indole group of the tryptophan-19 side chain. Although the binding site for this interaction is localized, the binding is weak for both anomers, with a binding free energy estimated as only ∼0.5 kcal/mol (i.e. near kBT). The face of the sugar stacked against the Trp indole ring is different for the two anomers of glucose, due to the disruption of the H1-H3-H5 hydrophobic triad of the beta anomer by the axial C1 hydroxyl group in the alpha anomer. The measurable affinity of the sugar for the Trp side chain is consistent with the very frequent occurrence of this group in the binding sites of proteins that complex with sugars. Proteins 2011; © 2011 Wiley-Liss, Inc.

U2 - 10.1002/prot.23047

DO - 10.1002/prot.23047

M3 - Article

C2 - 21574187

VL - 79 (7)

SP - 2224

EP - 2232

JO - Proteins: Structure, Function, and Bioinformatics

JF - Proteins: Structure, Function, and Bioinformatics

SN - 0887-3585

ER -