[Interaction of cationic surface-active antiseptics and serum albumin by the bacterial bioluminescence method]

Area of Science:

• Microbiology
• Biochemistry
• Pharmacology

Background:

• Cationic surface-active antiseptics are widely used for their antimicrobial properties.
• Interactions between antiseptics and biological molecules like human serum albumin (HSA) can alter their efficacy.
• Understanding these interactions is crucial for predicting antiseptic behavior in vivo.

Purpose of the Study:

• To investigate the binding of cationic surface-active antiseptics to human serum albumin.
• To determine the impact of albumin binding on the toxic and antibacterial characteristics of these antiseptics.
• To compare the binding affinity and effect on activity among different antiseptics.

Main Methods:

• Utilized a Photobacterium phosphoreum K3 strain isolated from the Black Sea for antimicrobial assays.
• Studied the binding of miramistine, ethonium, decametoxin, and chlorohexidine to human serum albumin.
• Assessed the changes in toxic and antibacterial properties post-albumin binding.

Main Results:

• Albumin binding caused the complete loss of toxic and antibacterial activity for miramistine, ethonium, and decametoxin.
• Chlorhexidine activity was reduced by 45-48% in the presence of albumin, indicating partial neutralization.
• Observed albumin binding capacities: miramistine (7.0-8.7%), ethonium (8.2-10%), and decametoxin (2.4-3%).

Conclusions:

• Human serum albumin significantly neutralizes the activity of several cationic surface-active antiseptics.
• Chlorhexidine exhibits a distinct interaction profile with albumin compared to miramistine, ethonium, and decametoxin.
• These findings highlight the importance of considering protein binding in the clinical application of antiseptics.