Protein Oligomerization 2.0

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
Dr. Marta Menegazzi
Guest Editors

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