Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 84, Issue 6, Pages 777-791Publisher
WILEY-BLACKWELL
DOI: 10.1002/prot.25025
Keywords
antimicrobial activity; Monte Carlo simulations; unstructured proteins; cationic protein; small angle X-ray scattering
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Funding
- Organizing Molecular Matter (OMM), Vinnova
- Vinnmer program
- Royal Physiographic Society in Lund
- Per-Eric and Ulla Schybergs Foundation
- Crafoord foundation
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Monte Carlo simulations and coarse-grained modeling have been used to analyze Histatin 5, an unstructured short cationic salivary peptide known to have anticandidical properties. The calculated scattering functions have been compared with intensity curves and the distance distribution function P(r) obtained from small angle X-ray scattering (SAXS), at both high and low salt concentrations. The aim was to achieve a molecular understanding and a physico-chemical insight of the obtained SAXS results and to gain information of the conformational changes of Histatin 5 due to altering salt content, charge distribution, and net charge. From a modeling perspective, the accuracy of the electrostatic interactions are of special interest. The used coarse-grained model was based on the primitive model in which charged hard spheres differing in charge and in size represent the ionic particles, and the solvent only enters the model through its relative permittivity. The Hamiltonian of the model comprises three different contributions: (i) excluded volumes, (ii) electrostatic, and (iii) van der Waals interactions. Even though the model can be considered as gross omitting all atomistic details, a great correspondence is obtained with the experimental results. (C) 2016 Wiley Periodicals, Inc.
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