The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …

Many proteins and peptides can form amyloid‐like structures both in vivo and in vitro.
Although strikingly similar fibrillar structures can be observed across a variety of amino acid …

Studies of proteins' formation of amyloid fibrils have revealed that potentially cytotoxic
oligomers frequently accumulate during fibril formation. An important question in the context …

Glucagon is a prominent peptide hormone, playing central roles in the regulation of glucose
blood-level and lipid metabolism. Formation of glucagon amyloid fibrils has been previously …

Glucagon and insulin maintain blood glucose homeostasis and are used to treat
hypoglycemia and hyperglycemia, respectively, in patients with diabetes. Whereas insulin is …

We report the transition dipole strengths and frequencies of the amyloid β-sheet amide I
mode for the aggregated proteins amyloid-β1–40, calcitonin, α-synuclein, and glucagon …

The skin-colonizing commensal bacterium Staphylococcus epidermidis is a leading cause of
hospital-acquired and device-related infections. Its pathogenicity in humans is largely due to …

Depending on external conditions, native proteins may change their structure and undergo
different association routes leading to a large scale polymorphism of the aggregates. This …

Osmolytes are small molecules that are exploited by cells as a protective system against
stress conditions. They favour compact protein states which makes them stabilize globular …

Ensembles of protein aggregates are characterized by a nano-and micro-scale
heterogeneity of the species. This diversity translates into a variety of effects that protein …