Protein Oligomerization 2.0

A special issue of Biophysica (ISSN 2673-4125).

Deadline for manuscript submissions: closed (16 March 2023) | Viewed by 2747

Special Issue Editors


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Guest Editor
Dipartimento Neurosci Biomed & Movimento, Università degli Studi di Verona, I-37134 Verona, Italy
Interests: investigations of protein structure and function and oligomerization; pancreatic-type Ribonucleases (RNase A, BS-RNase, Onconase) covalent or non-covalent oligomerization through 3D domain swapping; antitumor activity of covalent or domain-swapped RNase oligomers, in vitro and in mice; studies of the mechanism(s) of RNases oligomerization; investigations on the in vitro alpha-synuclein aggregation
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Guest Editor
Department of Neuroscience, Biomedicine and Movement Sciences, Biochemistry Section, University of Verona, Strada Le Grazie 8, 37134 Verona, Italy
Interests: natural products; inflammation; signal transduction; transcription factors; gene expression; antitumor therapy
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Protein oligomerization can occur either naturally or artificially, and can positively or negatively affect the properties of the native monomeric precursor.

The resulting oligomers can be small benign products, or larger amyloidogenic derivatives driving toward cross-beta fibrils that characterize neurodegenerative diseases.

The resulting species can be homo- or hetero-oligomers produced through artificial, or sometimes natural, intermolecular covalent cross-linking. Alternatively, they can be formed non-covalently (also naturally or artificially) through hydrophobic and/or electrostatic interactions, or following the so-called three-dimensional domain swapping (3D-DS) mechanism. These associations can occur as a consequence of modified environmental conditions, and the corresponding adducts can be stable or, sometimes, metastable.

Importantly, protein oligomerization can modify or light up the biological features of the native protein, or even switch-on properties lacked by the native monomer. This is particularly true for protein enzymes, whose self- or hetero-association can tune, properly or unwantedly, their activity.

This Special Issue welcomes the submission of original research papers and of reviews focused on data concerning one or more of the topics mentioned. The analysis and discussion of aspects connected with the possibility of better comprehending important features of human diseases and counteracting them are encouraged.

Dr. Giovanni Gotte
Prof. Dr. Marta Menegazzi
Guest Editors

Manuscript Submission Information

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Keywords

  • protein structure and function
  • natural/artificial, covalent/non-covalent protein oligomers
  • end-to-end stacking, hydrophobic/electrostatic protein oligomerization
  • three-dimensional domain swapping (3D-DS) mechanism
  • enzymatic activity of protein oligomers
  • biological benign/harmful properties of protein oligomers
  • signal transduction of protein oligomers
  • cytotoxic/antitumor activity of protein oligomers
  • neurodegenerative effects of protein oligomers
  • protein fibrillogenesis

Published Papers (1 paper)

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Review

12 pages, 859 KiB  
Review
Heterogeneous Tau Oligomers as Molecular Targets for Alzheimer’s Disease and Related Tauopathies
by Chih Hung Lo
Biophysica 2022, 2(4), 440-451; https://doi.org/10.3390/biophysica2040039 - 11 Nov 2022
Cited by 9 | Viewed by 2378
Abstract
Tauopathies, including Alzheimer’s disease (AD), are a group of neurodegenerative disorders characterized by pathological aggregation of microtubule binding protein tau. The presence of tau neurofibrillary tangles, which are insoluble β-sheet fibrils, in the brain has been the histopathological hallmark of these diseases as [...] Read more.
Tauopathies, including Alzheimer’s disease (AD), are a group of neurodegenerative disorders characterized by pathological aggregation of microtubule binding protein tau. The presence of tau neurofibrillary tangles, which are insoluble β-sheet fibrils, in the brain has been the histopathological hallmark of these diseases as their level correlates with the degree of cognitive impairment. However, recent studies suggest that tau oligomers, which are soluble proteins that are formed prior to insoluble fibrils, are the principal toxic species impairing neurons and inducing neurodegeneration. Targeting toxic tau oligomers is challenging, as they are mostly unstructured and adopting multiple conformations. The heterogeneity of tau oligomers is further illustrated by the different oligomeric species formed by various methods. The current models and technologies to study tau oligomerization represent important resources and avenues to push the forefront of elucidating the true toxic tau species. In this review, we will summarize the distinct tau oligomers generated using different strategies and discuss their conformational characteristics, neurotoxicity, relevance to pathological phenotypes, as well as their applications in drug discovery. This information will provide insights to understanding heterogeneous tau oligomers and their role as molecular targets for AD and related tauopathies. Full article
(This article belongs to the Special Issue Protein Oligomerization 2.0)
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