Differential scanning calorimetry of albumin solders: interspecies differences and fatty acid binding effects on protein denaturation.

Overview

BACKGROUND AND OBJECTIVE: Understanding albumin solder denaturation is important for laser tissue soldering. Human (HSA), bovine (BSA), porcine (PSA), and canine (CSA) albumin both fatty acid containing (FAC) and fatty acid free (FAF) were evaluated by using differential scanning calorimetry (DSC). STUDY DESIGN/MATERIALS AND METHODS: DSC was used to measure difference thermograms to determine the irreversible thermal denaturation profile for 50% albumin solutions. The denaturation transition's onset, end and peak temperatures, and enthalpy were measured. RESULTS: All FAC species, except BSA, exhibited twin peaked endotherms. Single endotherms were observed for all FAF species and BSA-FAC. Onset and end temperatures were significantly [P < 0.001] lower for all FAF species (except BSA's end temperature). There was a 30% decrease in the denaturation enthalpy between FAF and FAC groups. CONCLUSION: FAF albumin solders were found to denature at significantly lower temperatures, while also having a 30% reduction in enthalpy when compared with their FAC counterparts.