Universitá Degli Studi Di Siena

Setlance S.r.l.

Istituto Superiore Di Sanita

Luisa Bracci

Alessandro Pini

Chiara Falciani

Antonio Cassone

Luciano Polonelli

Paolo Neri

Leila Quercini

Neri Paolo

Luisa Lozzi

Jlenia Brunetti

Andrea Giuliani

Monica Fabbrini

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.

Methods for removing bacterial toxins from a biological fluid

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 andstrains. 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.

Antimicrobial peptide, branched forms thereof and their use in the treatment of bacteria infections

The present invention relates to an antibacterial peptide having from the amino to the carboxylic terminal an amino acid sequences selected from the group of: KKIRVRLSA, SEQ ID NO. 1, RRIRVRLSA, SEQ ID NO. 2, KRIRVRLSA, SEQ ID NO. 3, RKIRVRLSA, SEQ ID NO. 4 or a derivative thereof and uses thereof.

Peptide sequences, their branched form and use thereof for antimicrobial applications

Antibacterial peptides and their multimeric analogues, with a wide range of action and low haemolytic activity are described. In particular, the peptide molecules exhibit a high antimicrobial activity against numerous bacterial species, with reduced cytotoxicity and a low haemolysis rate. The molecules of the invention are advantageously usable as therapeutic agents and coadjutants against infections caused by strains that are resistant to common antibiotics.

Antibacterial peptides and analogues thereof

Anti-idiotypic antibodies which recognise the idiotope of an antibody specific for a yeast killer toxin possess microbicidal activity. Fragments (e.g. decapeptides) of these anti-idiotypic antibodies, particularly those comprising CDR residues, also show microbicidal activity, as do peptides having 5 the same sequence but composed of D-amino acids, or including amino acid substitutions. Peptidomimetics of these microbicidal polypeptides are also provided. Antiviral activity is also seen.

Toxin-related antibodies with antimicrobial and antiviral activity

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Siena, Italy

Luisa Bracci