Structural, kinetic, and thermodynamic aspects of insulin aggregation

Abstract

Given the significance of protein aggregation in proteinopathies and the development of therapeutic protein pharmaceuticals, revamped interest in assessing and modelling the aggregation kinetics has been observed. Quantitative analysis of...

Designing Multifunctional Biomaterials via Protein Self‐Assembly

“…From a general thermodynamic point of view, the driving force of the self‐assembly process is the minimization of the free energy of the system and this is achieved by increasing the attractive and decreasing the repulsive intermolecular interactions. In most self‐assembly processes, the formation of regular structures is determined by enthalpy, but it can also be controlled by entropy, and sometimes by both factors simultaneously [12–21] …”

“…For example, amyloid fibrils have been shown to represent one of the most stable thermodynamic states in the energy landscape. However, this does not exclude the fact that, depending on the external conditions, the final structures can be metastable, which determines the polymorphism of the resulting structures [12–21] …”

“…In most self-assembly processes, the formation of regular structures is determined by enthalpy, but it can also be controlled by entropy, and sometimes by both factors simultaneously. [12][13][14][15][16][17][18][19][20][21] Protein folding is one example of static self-assembly, according to the classification of G. Whitesides and B. Grzybowski [12] It is a complex process caused by hydrophobic interactions, intramolecular hydrogen bonds, van der Waals forces, electrostatic interactions, and environmental factors. Folding, as well as the formation of other ensembles and assemblies, can be described by an energy funnelshaped landscape, [14,15] which represents the energy of the system as a function of all possible conformations.…”

Designing Multifunctional Biomaterials via Protein Self‐Assembly

“…However, this does not exclude the fact that, depending on the external conditions, the final structures can be metastable, which determines the polymorphism of the resulting structures. [12][13][14][15][16][17][18][19][20][21] From a kinetic point of view, the formation of protein aggregates and self-assemblies occurs in different ways, with many intermediate products and is described by several models. [13,[22][23][24] Understanding this complex process has important implications for studying protein aggregationrelated diseases and the development of protein-based biomaterials.…”