DETAILED DESCRIPTION OF THE INVENTION Synthetic peptide P1 of the present invention is comprised by 26 amino acids.
The natural existence of this peptide in bacteria and animals has not been reported in the literature.
The data herein provided indicate that peptide P1 is a new bactericide factor.
In view of its proved antimicrobial activity against Gram-positive and Gram-negative bacteria, together with its ionophoric activity in the mitochondria, peptide P1 constitutes an antimicrobial peptide, taking into consideration that the term "antimicrobial" as it is used herein means that the peptide of the present invention can inhibit, prevent, or destroy the growth or multiplication of the microorganisms presented herein and others.
The term "contact" mentioned in the section of antimicrobial assays makes reference to the exposure of the bacteria to the peptide in such a way that the peptide permeabilizes effectively the outer membrane of the Gram-negative and Gram-positive bacteria, killing them.
The contact can be in vitro, for example, by means of the addition of the peptide to a bacterial culture in order to test the susceptibility of the bacteria to the peptide.
Examples of the bacteria, which can be killed or whose growth can be inhibited by means of peptide P1 include: Escherichia coli, Staphylococcus aureus, Streptococcus pneumoniae, Haemophilus influenzae, Enterococcus faecalis, Bacillus subtilis, Bacteroides fragilis and Clostridium perfringens, among others.
Peptide P1 has an amphipatic character, which allows it to form helicoidal structure when it is in the hydrophobic environment of the biological membranes.
The cationic charge (positive) of peptide P1 is determined by the amino acids located in the positions 6, 14, 18, 23 and 25, therefore, the total positive charges is "of plus five" (+5).
The residues of amino acids 6, 10, 14, 18, 19, 23, 25 and 26 are hydrophilic, while the residues of amino acids 1, 2, 3, 4, 5, 7, 8, 9, 11, 12, 13, 15, 16, 17, 20, 21, 22, 24 are all hydrophobic residues
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