The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …

Proteins at interfaces play important roles in cell biology, immunology, bioengineering, and
biomimetic material design. Many biological processes are based on interfacial protein …

Irreversible protein aggregation is problematic in the biotechnology industry, where
aggregation is encountered throughout the lifetime of a therapeutic protein, including during …

α-Synuclein is the major component of Lewy bodies and Lewy neurites, which are granular
and filamentous protein inclusions that are the defining pathological features of several …

Biofilm formation is a social behaviour that generates favourable conditions for sustained
survival in the natural environment. For the Gram‐positive bacterium B acillus subtilis the …

Increasing evidence indicates that many peptides and proteins can be converted in vitro into
highly organised amyloid structures, provided that the appropriate experimental conditions …

Amyloid fibrils and prions are proteinaceous aggregates that are based on a unique form of
polypeptide configuration, termed cross‐β structure. Using a group of chemically distinct …

The pressure–temperature phase diagram of various biomolecules is reviewed. Special
attention is focused on the elliptic phase diagram of proteins. The phenomenological …

Elastin provides extensible tissues, including arteries and skin, with the propensity for elastic
recoil, whereas amyloid fibrils are associated with tissue-degenerative diseases, such as …

Based on atomic force microscopy analysis of the morphology of fibrillar species formed
during fibrillation of α-synuclein, insulin, and the B1 domain of protein G, a previously …