Long COVID: From olfactory dysfunctions to viral Parkinsonism.

Neurological and psychiatric complications continue to be a public health concern in long coronavirus disease 2019 (COVID-19). This varies from olfactory dysfunctions such as parosmia to cognitive and emotional challenges. Historically, the surge of neurological disorders followed the viral pandemics, for example, the emergence of Encephalitis Lethargica after the outbreak of Spanish Influenza.

Tryptophan-cardanol fluorescent nanoparticles inhibit α-synuclein aggregation and disrupt amyloid fibrils.

Protein misfolding and aggregation play a vital role in several human diseases such as Parkinson's, Alzheimer's, and prion diseases. The development of nanoparticles that modulate aggregation could be potential drug candidates for these neurodegenerative disorders. Parkinson's disease pathogenesis is closely associated with the accumulation of α-synuclein oligomers and fibrils in the substantia nigra of the brain.

Self-assembly of novel Fmoc-cardanol compounds into hydrogels - analysis based on rheological, structural and thermal properties.

Hydrogels of low molecular weight molecules are particularly appealing for various biomedical applications such as drug delivery, tissue engineering, and antitumor therapy due to their excellent biocompatibility, biodegradability, and easy availability. Fmoc-peptide hydrogels form an essential category of these hydrogels. Herein we report a new class of Fmoc hydrogels in which cardanol (3-pentadecyl phenol (PDP)) is covalently linked with fluorenylmethyloxycarbonyl group.

Effect of the Interaction of the amyloid β (1-42) peptide with short single-stranded synthetic nucleotide sequences: morphological characterization of the inhibition of fibrils formation and fibrils disassembly.

The formation of extracellular neuritic plaques in the brain of individuals who suffered from Alzheimer's disease (AD) is a major pathological hallmark. These plaques consist of filamentous aggregates of the amyloid beta (1-42) (Aβ42) proteins. Prevention or reduction of the formation of these fibrils is foreseen as a potential therapeutic approach.

Label-free, optical sensing of the supramolecular assembly into fibrils of a ditryptophan-DNA hybrid.

The grafting of a short nucleic acid strand to ditryptophan dipeptide (WW) results in a peptide-DNA hybrid, which assembles into fibrils under controlled aggregation conditions as evidenced by label free optical sensing owing to the intrinsic fluorescence of the dipeptide.