Publication Date:
1993-01-15
Description:
Endotoxin [lipopolysaccharide (LPS)], the major antigen of the outer membrane of Gram-negative bacteria, consists of a variable-size carbohydrate chain that is covalently linked to N,O-acylated beta-1,6-D-glucosamine disaccharide 1,4'-bisphosphate (lipid A). The toxic activity of LPS resides in the lipid A structure. The structural features of synthetic peptides that bind to lipid A with high affinity, detoxify LPS in vitro, and prevent LPS-induced cytokine release and lethality in vivo were defined. The binding thermodynamics were comparable to that of an antigen-antibody reaction. Such synthetic peptides may provide a strategy for prophylaxis and treatment of LPS-mediated diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rustici, A -- Velucchi, M -- Faggioni, R -- Sironi, M -- Ghezzi, P -- Quataert, S -- Green, B -- Porro, M -- New York, N.Y. -- Science. 1993 Jan 15;259(5093):361-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biosynth Research Laboratories, Siena, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8420003" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Binding, Competitive
;
Bordetella pertussis/chemistry
;
Escherichia coli/chemistry
;
Hydrogen-Ion Concentration
;
Limulus Test
;
Lipid A/chemistry/*metabolism/toxicity
;
Lipopolysaccharides/chemistry/*metabolism/toxicity
;
Mice
;
Mice, Inbred BALB C
;
Micelles
;
Microscopy, Electron
;
Molecular Sequence Data
;
Peptides/chemical synthesis/chemistry/*metabolism
;
Polymyxin B/chemistry/*metabolism
;
Protein Conformation
;
Temperature
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
Permalink
