Nanoencapsulation of an active peptidic fraction from sea bream scales collagen.

Sea bream scales were subjected to enzymatic hydrolysis with Esperase, and a peptide fraction with a molecular mass <3kDa (F3) was isolated by ultrafiltration. F3 was encapsulated in nanoliposomes made of partially purified phosphatidylcholine (PC). Concentrations of 3.

Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis has an elongated shape which allows its interaction with both N- and M-domains of Hsp90.

The Hsp90 molecular chaperone is essential for protein homeostasis and in the maturation of proteins involved with cell-cycle control. The low ATPase activity of Hsp90 is critical to drive its functional cycle, which is dependent on the Hsp90 cochaperones. The Activator of Hsp90 ATPase-1 (Aha1) is a protein formed by two domains, N- and C-terminal, that stimulates the Hsp90 ATPase activity by several folds.