Significance of Artificial Intelligence in the Study of Virus-Host Cell Interactions.

A highly critical event in a virus's life cycle is successfully entering a given host. This process begins when a viral glycoprotein interacts with a target cell receptor, which provides the molecular basis for target virus-host cell interactions for novel drug discovery. Over the years, extensive research has been carried out in the field of virus-host cell interaction, generating a massive number of genetic and molecular data sources.

Self-assembling properties of peptides derived from TDP-43 C-terminal fragment.

Two highly fibrillogenic peptide sequences (MNFGAFSINP and EDLIIKGISV) were previously reported in the C-terminal fragment (CTF) of TDP-43 (220-414), a protein recently implicated in neuro-degenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-U). It was observed that the sequences MNFGAFS and EDLIIKG harbor their respective fibrillogenic domains. Here, the self-assembling properties of peptides obtained by systematic deletion of residues from these two sequences were investigated with the help of light scattering, thioflavin T fluorescence, transmission electron microscopy, and circular dichroism spectroscopy.

Delineation of the core aggregation sequences of TDP-43 C-terminal fragment.

Ubiquitinated cytoplasmic inclusions of TDP-43 and its C-terminal cleavage products are the pathological hallmarks of amyotrophic lateral sclerosis and frontotemporal lobar degeneration with ubiquitinated inclusions. The C-terminal fragments (CTFs) of TDP-43 are increasingly considered to play an important role in its aggregation and in disease. Here, we employed a set of synthetic peptides spanning the length of the TDP-43 CTF (220-414) in order to find out its core aggregation domains.