Self-assembly and aggregation of proteins
Section snippets
Major recent advances
On the level of single peptides the influence of chemical groups on fibrillisation is being studied, elaborating on recent advances in X-ray microcrystallography. On the level of proteins the various pathways towards fibrillisation are being unraveled including the influence of protein hydrolysis.
Linear structures: amyloids and amyloid-like assemblies
Amyloid fibrils (related to disease) and amyloid-like fibrils share some structural properties, such as the presence of β-sheets orthogonal to the fibril axis. Knowledge of the mechanisms of amyloid(-like) formation leading to predictive models is desirable, in particular on a structural molecular level. This is necessary in order to prevent amyloidosis, as nicely reviewed by Sciaretta et al. [1], as well as in order to utilize amyloid-like fibrils. Fibrils can be utilized as gelling materials,
Spherulites
A spherulite is a spherical ordered structure that results in a Maltese extinction pattern when observed between crossed polarisers through a light microscope. Spherulite formation also is observed during polymer crystallisation and during crystallisation of metals. Several proteins which are reported to exhibit such structures, which range up to millimetres in size. They include bovine insulin [62] and β-lactoglobulin [63], [64]. Interestingly, two peptides, one being cyclic and one being
Conclusions
Since the assembly of proteins is ubiquitous, the subject receives a considerable attention from various disciplines. Many different structures, varying in size as well as in shape, can be formed depending on the exact conditions when they are formed. This leads to the opportunity to engineer structures with certain desirable properties. Linear structures like amyloids and amyloid-like fibrils form an interesting class for studying for their importance in the medical field, but also have
Acknowledgement
We gratefully acknowledge the assistance of Mrs. E. Jansen in the preparation of the manuscript.
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