Modulation of amyloid fibrillation of bovine β-lactoglobulin by selective methionine oxidation.

Deposition of oxidation-modified proteins during normal aging and oxidative stress are directly associated with systemic amyloidoses. Methionine (Met) is believed to be one of the most readily oxidisable amino acid residues of protein. Bovine beta-lactoglobulin (β-lg), a model globular whey protein, has been presented as a subsequent paradigm for studies on protein aggregation and amyloid formation.

Insight into the co-solvent induced conformational changes and aggregation of bovine β-lactoglobulin.

Many proteins form ordered irreversible aggregates called amyloid fibrils which are responsible for several neurodegenerative diseases. β-lactoglobulin (β-lg), an important globular milk protein, self-assembles to form amyloid-like fibrils on heating at low pH. The present study investigated the effects of two commonly used organic solvents acetonitrile (MeCN) and antimicrobial preservative benzyl alcohol (BA) on the conformation and self-assembly of β-lg at ambient condition.

Amyloid fibril formation by β-lactoglobulin is inhibited by gold nanoparticles.

The endogenous deposition of protein fibrillar aggregates in the tissues is the cause of several neurodisorders. In the present study the native β-lactoglobulin (β-lg) has been driven towards amyloid fibrillar aggregates when it was exposed to heat at 75°C for 1h at pH 7.5.

Tryptophan dynamics in the exploration of micro-conformational changes of refolded β-lactoglobulin after thermal exposure: a steady state and time-resolved fluorescence approach.

Refolding intermediates of proteins, including molten globules, are likely to undergo dynamic conformational transitions. In this work, thermal unfolding and refolding of bovine β-lactoglobulin (β-lg) have been revisited to encounter such intermediate states. Lower thermal range (< 80°C) was selected to avoid irreversible aggregate formation.

Unfolding diminishes fluorescence resonance energy transfer (FRET) of lysine modified β-lactoglobulin: Relevance towards anti-HIV binding.

In accordance with the recent reports by Ng et al. (2001) [12] and Pellengrini et al. (2001) [13], that acetylated and succinylated β-lg has a potent HIV-I and HIV-II type enzyme inhibitory activity, a spectro-fluoremetric approach has been made to understand the mode of interactions playing the key role in inhibition process.