Synthesis and antibacterial activity of new peptides from Alfalfa RuBisCO protein hydrolysates and mode of action via a membrane damage mechanism against Listeria innocua. (February 2018)

• Record Type: Journal Article
• Authors: Kobbi, Sabrine; Nedjar, Naima; Chihib, Nourdine; Balti, Rafik; Chevalier, Mickael; Silvain, Amandine; Chaabouni, Semia; Dhulster, Pascal; Bougatef, Ali
• Is Part Of: Microbial pathogenesis. Volume 115(2018)
• Page Start: 41
• Page End: 49
• Publication Date: 2018-02
• Subjects: RuBisCO -- Antibacterial peptides -- Mode of action -- Membrane permeability -- Listeria innocua; Pathogenic microorganisms -- Periodicals; Pathology, Molecular -- Periodicals; Communicable Diseases -- microbiology -- Periodicals; Communicable Diseases -- parasitology -- Periodicals; Micro-organismes pathogènes -- Périodiques; Pathologie moléculaire -- Périodiques; Electronic journals; 616.9041
• DOI: 10.1016/j.micpath.2017.12.009
• Languages: English
• ISSNs: 0882-4010

Abstract

Abstract: In this work we evaluated the mode of action of six new synthesized peptides (Met-Asp-Asn ;Glu-leu-Ala-Ala-Ala-Cys; Leu-Arg-Asp-Asp-Phe; Gly-Asn-Ala-Pro-Gly-Ala-Val-Ala; Ala-Leu-Arg-Met-Ser-Gly andArg-Asp-Arg-Phe–Leu ), previously identified, from the most active peptide fractions of RuBisCO peptic hydrolysate against Listeria innocua via a membrane damage mechanism. Antibacterial effect and the minimum inhibitory concentrations (MIC) of these peptides were evaluated against six strains and their hemolytic activities towards bovine erythrocytes were determined. Prediction of the secondary structure of peptides indicated that these new antibacterial peptides are characterized by a short peptide chains (3–8 amino acid) and a random coli structure. Moreover, it was observed that one key characteristic of antibacterial peptides is the presence of specific amino acids such as cysteine, glycine, arginine and aspartic acid. In addition the determination of the extracellular potassium concentration revealed that treatment with pure RuBisCO peptides could cause morphological changes of L. innocua and destruction of the cell integrity via irreversible membrane damage. The results could provide information for investigating the antibacterial model of antibacterial peptides derived from RuBisCO protein hydrolysates. Highlights: Antibacterial activity of new peptides from RubisCO proteins was studied. The minimum inhibitory concentrations toward six strains were determined. The hemolytic activity toward bovine erythrocytes was determined. The mode of action against Listeria innocua was determined. Treatment with pure RuBisCO peptides cause destruction of the cell integrity via irreversible membrane damage.