Chemical studies on polymyxin B.
نویسندگان
چکیده
منابع مشابه
Contribution of each amino acid residue in polymyxin B(3) to antimicrobial and lipopolysaccharide binding activity.
This study on the structure-activity relationship of polymyxin B, a cyclic peptide antibiotic, used sixteen synthetic polymyxin B(3) analogs including alanine scanning analogs to elucidate the contribution of the side chains to antimicrobial activity and lipopolysaccharide (LPS) binding. Of these analogs, [Ala(5)]-polymyxin B(3) showed greatly reduced antimicrobial activity against Escherichia ...
متن کاملMimicking an antimicrobial peptide polymyxin B by use of cyclodextrin.
Cyclodextrin derivatives prepared to mimic a membrane active antibacterial peptide polymyxin B strongly permeabilized bacterial membrane and inhibited bacterial proliferation.
متن کاملبررسی اثر سینرژیسمی آنتی‌بیوتیک‌های پلی‌میکسین B سولفات و تری متوپریم بر یرسینیاانتروکلی‌تیکا و دیگر گونه‌های وابسته
Background and Objectives: Previous studies have shown that polymyxin B sulfate and trimthoprim antibiotics are not individually effective on Yersinia enterocolitica and their closely related species. The aim of this study was to evaluate the synergistic effect of above antibiotics on Y. enterocolitica and their closely related species, from the clinical and the natural environment specimen col...
متن کاملPolymyxin B and rifampin: new regimen for multiresistant Serratia marcescens infections.
Polymyxin B and rifampin were given to 12 patients with multi-drug-resistant nosocomial Serratia marcescens infections. Eight cures were achieved; drug hepatotoxicity occurred once; one fatal suprainfection was encountered; and two patients died during therapy of causes related to severe underlying illnesses. Polymyxin B and rifampin were uniformly synergistic in vitro against the infecting str...
متن کاملIsolation, structural characterization, and properties of mattacin (polymyxin M), a cyclic peptide antibiotic produced by Paenibacillus kobensis M.
Mattacin is a nonribosomally synthesized, decapeptide antibiotic produced by Paenibacillus kobensis M. The producing strain was isolated from a soil/manure sample and identified using 16 S rRNA sequence homology along with chemical and morphological characterization. An efficient production and isolation procedure was developed to afford pure mattacin. Structure elucidation using a combination ...
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ورودعنوان ژورنال:
- The Journal of clinical investigation
دوره 28 5 Pt 1 شماره
صفحات -
تاریخ انتشار 1949