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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Heldt, Caryn L. Zahid, Amna Vijayaragavan, K. Saagar Mi, Xue |
| Description | Author Affiliation: Heldt CL ( Department of Chemical Engineering, Michigan Technological University, 1400 Townsend Dr., Houghton, MI 49931, USA. Electronic address: heldt@mtu.edu.); Zahid A ( Department of Chemical Engineering, Michigan Technological University, 1400 Townsend Dr., Houghton, MI 49931, USA.); Vijayaragavan KS ( Department of Chemical Engineering, Michigan Technological University, 1400 Townsend Dr., Houghton, MI 49931, USA.); Mi X ( Department of Chemical Engineering, Michigan Technological University, 1400 Townsend Dr., Houghton, MI 49931, USA.) |
| Abstract | The physical characteristics of viruses needs to be understood in order to manipulate the interaction of viruses with host cells, as well as to create specific molecular recognition techniques to detect, purify, and remove viruses. Viruses are generally believed to be positively charged at physiological pH, but there are few other defining characteristics. Here, we have experimentally and computationally demonstrated that a non-enveloped virus is more hydrophobic than a panel of model proteins. Reverse-phase and hydrophobic interaction chromatography and ANS fluorescence determined the experimental hydrophobic strength of each entity. Computational surface hydrophobicity was calculated by the solvent exposed surface area of the protein weighted by the hydrophobicity of each amino acid. The results obtained indicate a strong correlation between the computational surface hydrophobicity and experimentally determined hydrophobicity using reverse-phase chromatography and ANS fluorescence. The surface hydrophobicity did not compare strongly to the weighted average of the amino acid sequence hydrophobicity. This demonstrates that our simple method of calculating the surface hydrophobicity gives general hydrophobicity information about proteins and viruses with crystal structures. In the process, this method demonstrated that porcine parvovirus (PPV) is more hydrophobic than the model proteins used in this study. This adds an additional dimension to currently known virus characteristics and can improve our manipulation of viruses for gene therapy targeting, surface adsorption and general understanding of virus interactions. |
| File Format | HTM / HTML |
| ISSN | 09277765 |
| Journal | Colloids and Surfaces B: Biointerfaces |
| Volume Number | 153 |
| e-ISSN | 18734367 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2017-02-13 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Content Type | Text |
| Resource Type | Article |
| Subject | Colloid and Surface Chemistry Medicine Physical and Theoretical Chemistry Surfaces and Interfaces Biotechnology |
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