Spectroscopy data of ceftriaxone-lysozyme interaction and computational studies.

The data article presents the results obtained from fluorescence and synchrotron radiation circular dichroism spectroscopies about the lysozyme-ceftriaxone interaction at neutral and acidic pH values as well as the computational calculations described in the accompanying research article (Ruzza et al., sub) [1].

Chaperone-like effect of ceftriaxone on HEWL aggregation: A spectroscopic and computational study.

Background: Lysozyme is a widely distributed enzyme present in a variety of tissue and body fluids. Human and hen egg white lysozyme are used as validated model to study protein folding and stability and to understand protein misfolding and aggregation. We recently found that ceftriaxone, a β-lactam antibiotic able to overcome the blood-brain barrier, successfully eliminated the cellular toxic effects of misfolded proteins as Glial Fibrillary Acidic Protein (GFAP) and α-synuclein.