Abstract: Methods for removing bacterial toxins such as lipopolysaccharide and lipoteichoic acid from a biological fluid with a peptide selected from KKIRVRLSA (SEQ ID NO:1), RRIRVRLSA (SEQ ID NO:2), KRIRVRLSA (SEQ ID NO:3) and RKIRVRLSA (SEQ ID NO:4), the peptide being covalently attached to a solid support through the C-terminus, optionally with the interposition of a linker.
Abstract: This invention relates to methods for removing bacterial toxins such as lipopolysaccharide and lipoteichoic acid from a biological fluid. In such method a peptide, selected from the list of KKIRVRLSA, RRIRVRLSA, KRIRVRLSA and RKIRVRLSA, is covalently attached to a solid support through its C-terminus, optionally with the interposition of a linker, and is used to capture the toxins. This invention also relates to such derivatised solid supports and to cartridges, columns, and medical apparatuses comprising such derivatised solid supports.
Abstract: There are disclosed therapeutic combinations of an antibacterial peptide and an antibiotic drug for use in the treatment of infections caused by Gram-negative pathogens, including bacterial strains resistant to common antibiotics. Also disclosed are pharmaceutical preparations and compositions containing the antibacterial peptide and antibiotics.
Abstract: The instant invention refers to an antibacterial peptide with all amino acids in D-configuration, possessing strong antimicrobial activity against Gram-negative and Gram-positive bacteria and Candida strains. The peptide can be in linear form multimerised on a skeleton of polyacrylamide, of dextrane units or on a skeleton of ethylene glycol units. The peptide is resistant proteolysis especially when synthesized in the tetra-branched form where identical peptide sequences are linked together by an appropriate molecular scaffold.
Abstract: The instant invention refers to an antibacterial peptide with all aminoacids in D-configuration, possessing strong antimicrobial activity against Gram-negative and Gram-positive bacteria and Candida strains. The peptide can be in linear form or multimerised on a skeleton of polyacrylamide, of dextrane units or on a skeleton of ethylene glycol units. The peptide is resistant to proteolysis especially when synthesized in the tetra-branched form where identical peptide sequences are linked together by an appropriate molecular scaffold.