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Dodine as a protein denaturant: the best of two worlds?

ABSTRACT: Traditional denaturants such as urea and guanidinium ion unfold proteins in a cooperative "all-or-none" fashion. However, their high working concentration in combination with their strong absorption in the far ultraviolet region make it impossible to measure high quality circular dichroism or infrared spectra, which are commonly used to detect changes in protein secondary structure. On the other hand, detergents such as dodecyl sulfate destabilize native protein conformation at low millimolar concentrations and are UV transparent, but they denature proteins more gradually than guanidinium or urea. In this work, we studied the denaturation properties of the fungicide dodecylguanidinium acetate (dodine), which combines both denaturants into one. We show that dodine unfolds some small proteins at millimolar concentrations, facilitates temperature denaturation, and is transparent enough at its working concentration, unlike guanidinium, to measure full range circular dichroism spectra. Our results also suggest that dodine allows fine-tuning of the protein's unfolded state, unlike traditional "all-or-none" denaturants.

SUBMITTER: Gelman H

PROVIDER: S-EPMC3834592 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature

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Dodine as a protein denaturant: the best of two worlds?

Gelman Hannah H Perlova Tatyana T Gruebele Martin M

The journal of physical chemistry. B 20130816 42

Traditional denaturants such as urea and guanidinium ion unfold proteins in a cooperative "all-or-none" fashion. However, their high working concentration in combination with their strong absorption in the far ultraviolet region make it impossible to measure high quality circular dichroism or infrared spectra, which are commonly used to detect changes in protein secondary structure. On the other hand, detergents such as dodecyl sulfate destabilize native protein conformation at low millimolar co ...[more]

PMID: 23906507

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Project description:PurposeTo allow for comprehensive noninvasive diagnostics of coronary artery disease (CAD) by using three-dimensional (3D) image fusion of CT coronary angiography, CT-derived fractional flow reserve (CT FFR), whole-heart dynamic 3D cardiac MRI perfusion, and 3D cardiac MRI late gadolinium enhancement (LGE).Materials and methodsSeventeen patients (54 years ± 10 [standard deviation], one female) who underwent cardiac CT and cardiac MRI were included (combined subcohort of three prospective trials). Software facilitating multimodal 3D image fusion was developed. Postprocessing of CT data included segmentation of the coronary tree and heart contours, calculation of CT FFR values, and color coding of the coronary tree according to CT FFR. Postprocessing of cardiac MRI data included segmentation of the left ventricle (LV) in cardiac MRI perfusion and cardiac MRI LGE, co-registration of cardiac MRI to CT data, and projection of cardiac MRI perfusion and LGE values onto the high spatial resolution LV from CT.ResultsImage quality was rated as good to excellent (scores: 2.5-2.6; 3 = excellent). CT coronary angiography revealed significant stenoses in seven of 17 cases (41%). CT FFR was possible in 16 of 17 cases (94%) and showed pathologic flow in seven of 17 cases (41%), six of which coincided with cases revealing significant stenoses at CT coronary angiography. Cardiac MRI perfusion identified eight of 17 patients (47%) with hypoperfusion (ischemic burden of 17% ± 5). Cardiac MRI LGE showed myocardial scar in three of 17 cases (18%, scar burden of 7% ± 4). Conventional two-dimensional readout of CT coronary angiography and cardiac MRI resulted in eight of 17 cases (47%) with uncertain findings. Most of these divergent findings could be solved when adding information from CT FFR and 3D image fusion (six of eight, 75%).ConclusionMultimodal 3D cardiac image fusion is feasible and may help with comprehensive noninvasive CAD diagnostics.Supplemental material is available for this article.© RSNA, 2020.

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Dodine as a protein denaturant: the best of two worlds?

Publications

Dodine as a protein denaturant: the best of two worlds?

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