Background The demonstration of chaperone-like activity in peptides (mini-chaperones)
derived from α-crystallin's chaperone region has generated significant interest in exploring …

The chaperone and anti-apoptotic activity of α-crystallins (αA-and αB-) and their derivatives
has received increasing attention due to their tremendous potential in preventing cell death …

Small heat-shock proteins (sHsps), such as αB-crystallin, are one of the major classes of
molecular chaperone proteins. In vivo, under conditions of cellular stress, sHsps are the …

Amyloid fibril formation occurs from a wide range of peptides and proteins and is typically
associated with a loss of protein function and/or a gain of toxic function, as the native …

α-Crystallin is the archetypical chaperone of the small heat-shock protein family, all
members of which contain the so-called “α-crystallin domain”(ACD). This domain and the N …

During its life cycle, a cell can be subjected to various external negative effects. Many
proteins provide cell protection, including small heat shock proteins (sHsp) that have …

Melittin, the most potent pharmacological ingredient of honey bee venom, induces
haemolysis, lymphocyte lysis, long-term pain, localised inflammation, and hyperalgesia. In …

Many of the newly discovered therapeutic peptides and molecules are limited by their
inability to cross the cell membrane. In the present study, a cell‐penetrating peptide (CPP) …

The highly conserved alpha crystallin domain of the small heat shock proteins is essential
for dimerization and also implicated in substrate interaction. In this study, we designed four …

We report the first small molecule peptides based on the N-terminal sequence of heat shock
protein 27 (Hsp27, gene HSPB1) that demonstrates chaperone-like activity. The peptide …