Dean Edun's research while affiliated with University of Notre Dame and other places
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Publications (13)
Significance
Phenol soluble modulins (PSMs) are an important class of peptides secreted by Staphylococcus aureus bacteria. The toxicity to human cells and unique ability of one such peptide, PSMα3, to aggregate into an α-helical amyloid-like structure may hold a key to a better understanding of the virulence of dangerous pathogens such as methicill...
The coupled amide-I vibrational modes in peptide systems such as fibrillar aggregates can often provide a wealth of structural information, though the associated spectra can be difficult to interpret. Using exciton scattering calculations, we characterized the polarization selective 2DIR peak patterns for cross-α peptide fibrils, a challenging syst...
The coupled amide-I vibrational modes in peptide systems such as fibrillar aggregates can often provide a wealth of structural information, though the associated spectra can be difficult to interpret. Using exciton scattering calculations, we characterized the polarization selective 2DIR peak patterns for cross-α peptide fibrils, a challenging syst...
The coupled amide-I vibrational modes in peptide systems such as fibrillar aggregates can often provide a wealth of structural information, though the associated spectra can be difficult to interpret. Using exciton scattering calculations, we characterized the polarization selective 2DIR peak patterns for cross-α peptide fibrils, a challenging syst...
The formation of ordered cross-β amyloid protein aggregates is associated with a variety of human disorders. While conventional infrared methods serve as sensitive reporters of the presence of these amyloids, the recently discovered amyloid secondary structure of cross- fibrils presents new questions and challenges. Herein, we report results using...
The formation of ordered cross-β amyloid protein aggregates is associated with a variety of human disorders. While conventional infrared methods serve as sensitive reporters of the presence of these amyloids, the recently discovered amyloid secondary structure of cross- fibrils presents new questions and challenges. Herein, we report results using...
The formation of ordered cross-β amyloid protein aggregates is associated with a variety of human disorders. While conventional infrared methods serve as sensitive reporters of the presence of these amyloids, the recently discovered amyloid secondary structure of cross- fibrils presents new questions and challenges. Herein, we report results using...
The formation of ordered cross-β amyloid protein aggregates is associated with a variety of human disorders. While conventional infrared methods serve as sensitive reporters of the presence of these amyloids, the recently discovered amyloid secondary structure of cross- fibrils presents new questions and challenges. Herein, we report results using...
The formation of ordered cross-β amyloid protein aggregates is associated with a variety of human disorders. While conventional infrared methods serve as sensitive reporters of the presence of these amyloids, the recently discovered amyloid secondary structure of cross- fibrils presents new questions and challenges. Herein, we report results using...
The formation of ordered cross-β amyloid protein aggregates is associated with a variety of human disorders. While conventional infrared methods serve as sensitive reporters of the presence of these amyloids, the recently discovered amyloid secondary structure of cross- fibrils presents new questions and challenges. Herein, we report results using...
Proline-arginine (PR) dipeptide repeats have been shown to undergo liquid-liquid phase separation and are an example of a growing number of intrinsically disordered proteins that can assemble into membraneless organelles. These structures have been posited as a nucleation site for pathogenic protein aggregation. As such, a better understanding of t...
p>Proline-arginine (PR) dipeptide repeats have been shown to undergo liquid-liquid phase separation and are an example of a growing number of intrinsically disordered proteins that can assemble into membraneless organelles. These structures have been posited as a nucleation site for pathogenic protein aggregation. As such, a better understanding of...
Wide-field imaging through dielectric microspheres has emerged in recent years as a simple and effective approach for generating super-resolution images at visible wavelengths. We present, to our knowledge, the first demonstration that dielectric microspheres can be used in a wide-field infrared (IR) microscope to enhance the far field resolution....
Citations
... Limited, yet seminal, works have bubbled up to rationalize the observed functionalities of PSMα3 based on its structure, e.g., characterization of the monomeric state, 6 factors stabilizing the mature fibril, 7−9 the kinetics of aggregation, 10−13 nature/location-, 14−16 length-, 16−19 structure-, 19,20 and phasespecific 5,15,21,22 roles of the constituting residues in diverse functionalities of the peptide, and membrane interaction with PSMα3. 14,23 However, the nascent phase of the research is filled with contradictory observations producing inconclusive inferences on the structure of the fibrillar state, 3,5,14,24,25 the factors required for cytotoxicity, 3−5,14,23,26−30 sequence/ structure-encoded functional specificity, 6 and salt concentration dependence of the structure−toxicity relationship. 21,31 The lack of a comprehensive description of the deleterious aggregation process has motivated the present study, which focuses on the switching of specific roles of the charged and the hydrophobic residues at different stages of the aggregation pathway by a comparative kinetic−thermodynamic analysis between the wild-type (WT) PSMα3 sequence and three designed variants with isoleucine to model operatively increased hydrophobicity (WT → IMT, F/V/L < I), glutamine to model lack of charge with comparable hydrophilicity (WT → QMT, D/E/K ≈ Q), and proline to model moderately less hydrophilicity with one less charged residue (WT → PMT, D > P) mutations 32 (see Supporting Information, justification behind the modeling of noncanonical mutants, Figures S1 and S2) at a low salt concentration (see Supporting Information, rationalization behind the choice of low salt concentration). ...
... 73,74 Recent studies have highlighted the strong interplay between transient secondary structures and phase separation behaviors. [75][76][77][78] For instance, IDPs and IDRs often adopt more extended conformations within condensates and often with an increased propensity for β-structures. [79][80][81] It has also suggested LLPS can induce the folding of poly-(PR) peptides into helical conformations, 77,82 which is a characteristic feature of aging-related phase transition pathologies. ...
... Newer designs are still being sought including, for example, a proposed structured illumination in a wide field geometry that has been proposed but not implemented 48 and the recent report of dielectric microspheres for resolution improvement in the IR. 49 An alternative may be a completely computational approach via deep learning that has been demonstrated for linear fluorescence microscopy. 50 The strength of TAM to acquire information across spatial, temporal, and spectral dimensions also represents one of its greatest weaknesses for collecting data in reasonable timeframes. ...
