Persistence Dynamics of Antimicrobial-Resistant in the Pharynx of Rhesus Macaques.

Pharyngeal infections by are often asymptomatic, making them difficult to treat. However, animal modeling of human pharyngeal infections by pathogenic species is challenging due to numerous host tropism barriers. We have relied on rhesus macaques to investigate pharyngeal persistence of naturally occurring species in response to antibiotics.

The conformational epitope for a new Aβ42 protofibril-selective antibody partially overlaps with the peptide N-terminal region.

Aggregation and accumulation of amyloid-β peptide (Aβ) is a key component of Alzheimer's disease (AD). While monomeric Aβ appears to be benign, oligomers adopt a biologically detrimental structure. These soluble structures can be detected in AD brain tissue by antibodies that demonstrate selectivity for aggregated Aβ.

Aβ40 has a subtle effect on Aβ42 protofibril formation, but to a lesser degree than Aβ42 concentration, in Aβ42/Aβ40 mixtures.

Recent findings suggest that the senile plaques in Alzheimer's disease may contain soluble amyloid-β peptide (Aβ) fibril precursors along with insoluble fibrils. These soluble Aβ species, including oligomers and protofibrils, have been well-studied in vitro and are formed via non-covalent self-assembly of Aβ monomers. While both 40- and 42-residue forms of Aβ are observed in the human body, the majority of the Aβ aggregation work has been conducted on Aβ42 or Aβ40 separately, with relatively few investigations of mixtures.

Biophysical comparison of soluble amyloid-β(1-42) protofibrils, oligomers, and protofilaments.

Some of the pathological hallmarks of the Alzheimer's disease brain are senile plaques composed of insoluble amyloid-β protein (Aβ) fibrils. However, much of the recent emphasis in research has been on soluble Aβ aggregates in response to a growing body of evidence that shows that these species may be more neurotoxic than fibrils. Within this subset of soluble aggregated Aβ are protofibrils and oligomers.