Reports on Peptides and Proteins from Indian Institute of Technology Provide New Insights [Action of Caffeine as an Amyloid Inhibitor in the Aggregation of A beta(16-22) Peptides]
By a News Reporter-Staff News Editor at Life Science Weekly — A new study on Peptides and Proteins is now available. According to news reporting out of Gauhati, India, by NewsRx editors, research stated, “Alzheimer’s disease (AD) is a neurodegenerative disease caused due to aggregation of A beta peptides in the brain tissues. Recently, several studies on AD transgenic mice have shown the effect of caffeine in significantly reducing the A beta amyloid level in their brains.”
Our news journalists obtained a quote from the research from the Indian Institute of Technology, “However, the mechanism and mode of caffeine action on amyloid aggregation are not known. Therefore, in this study, we have carried out molecular dynamics simulations of five amyloicl-fOrming 16-22 peptides in pure water and in a regime of caffeine solutions, with different caffeine/peptide stoichiometric ratios. The secondary structure analyses _of peptides in pure- water show the formation of fl -sheet conformations, whereas on addition of caffeine, these ordered conformations become negligible. The radial distribution function, contact map, nonbonding interaction energy, hydrogen bonding, potential of mean force, and hydration analyses show. that there is less interpeptide interaction in the presence of caffeine, and the effect is greater with an increasing caffeine ratio. The interaction of aromatic phenylalanine residues of peptides with caffeine restricts the interpeptide interaction tendency. Upon increasing the number of caffeine molecules, interaction of caffeine with other hydrophobic residues also increases.”