Structural preconditions and inhibition methods of human serum albumin beta-lactamase activity
The present work is dedicated to the important problem of human blood serum factors impact on beta-lactams. Beta-lactamase activity - the integral property of human blood, is possessed by albumin fraction to 86-100%. Tertiary structure is necessary for presence of the specifi ed activity. Klavulanic acid and tazobactam are capable to reduce beta-lactamase activity of blood, possibly by its competitive inhibition that means presence of active site in a molecule of albumin that diff ers from bacterial class A beta-lactamase one. Docking of albumin and beta-lactam antibiotics and class A beta-lactamase inhibitors revealed the active site formed by the following amino acid residues: SER 192, LYS 195, GLN 196, LYS 199, and ARG 257. The given active site is responsible for interaction of albumin and all studied beta-lactam antibiotics and klavulanic acid. Sulbactam and tazobactam are placed in other site that explains their twice-smaller efficiency of inhibition in comparison with potassium klavulanate of similar concentration.