Comparative study of binding power of polymyxin B and its simulating peptide to lipopolysaccharides lipoid A.
- Author:
Zhi-xiang ZHU
1
;
Wei-ping LI
;
Li-yong ZHANG
;
Xiao-yun GONG
Author Information
- Publication Type:Journal Article
- MeSH: Cell Wall; chemistry; Endotoxins; Gram-Negative Bacteria; Lipopolysaccharides; chemistry; toxicity; Peptides; chemistry; pharmacology; Polymyxin B; chemistry; pharmacology
- From: Chinese Journal of Burns 2004;20(4):232-234
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo observe the binding power of polymyxin B (PMB) and its simulation peptide to lipopolysaccharide (LPS) and lipoid A.
METHODSLPS and lipoid A were separately coated on biosensor. 5 microl of PMB (0.01 microg/L) 5 microl of its simulating peptide 1 (PMBSP1 0.01 microg/L) and 5 microl of its simulating peptide 2 (PMBSP2, 0.01 microg/L) were respectively added into the hydrophobic sample pool. The combining power of PMB and its simulating peptides PMBSP1 and PMBSP2 to LPS and lipoid A was compared. RESULTS (1) PMBSP1 almost did not bind LPS and lipoid A, while PMB and PMBSP2 possessed high affinity with LPS and lipoid A. (2) The peak value (98.41 +/- 7.31) rad/s of PMBSP2 binding LPS was much higher than that (83.58 +/- 5.42) rad/s of PMB in binding LPS (P < 0.05). While the peak value of PMB in binding lipoid A was similar to that of PMBSP2. (3) The peak value of PMB binding LPS was significantly lower than that of PMB in binding lipoid A (P < 0.05). But there was no difference between the peak value of PMBSP2 in binding LPS and that of PMBSP2 in binding lipoid A. (4) PMBSP2 could bind to LPS and lipoid A in a shorter time to reach peak levels.
CONCLUSIONCompared with PMB, the PMBSP2 could bind to LPS and lipoid A in a shorter time. In addition, PMBSP2 exhibited similar affinity to LPS and lipoid A. This indicated that PMBSP might possess better anti-LPS activity due to its lack of space steric hindrance when PMBSP binding the lipoid A of LPS.
