Pullulan nanofibers containing the antimicrobial palindromic peptide LfcinB (21–25)_Palobtainedviaelectrospinning

Abstract

Pullulan nanofibers containing antimicrobial peptide derived from LfcinB an option as biomaterial for wound dressings.

Selective cytotoxic effect against the MDA-MB-468 breast cancer cell line of the antibacterial palindromic peptide derived from bovine lactoferricin

“…It is believed that the selectivity for cancer cells over normal cells is in part due to electrostatic interactions between the positively-charged peptide and the negatively-charged membrane components 10,11 such as phosphatidylserine, glycosylated mucins, sialylated gangliosides, sialic acid, and heparan sulphate in cancer cells. 12 The minimal motif with antibacterial and anticancer activity has been identied as LfcinB (20)(21)(22)(23)(24)(25): RRWQWR. This sequence is amphipathic and positively charged.…”

Delivery of streptomycin to the rat colon by use of electrospun nanofibers

“…In line with our observations, core–shell fibers, which are produced by coaxial electrospinning, have previously shown successful sustained release of hydrophilic drugs such as streptomycin 28 . Regarding drug delivery applications using pullulan nanofibers, there are several studies focusing on fast dissolving properties of pullulan and recommending it for fast delivery approaches via the buccal route 8 , 19 , 29 , 30 or for wound dressing applications 6 , 31 . Our findings suggest that antibiotic-loaded pullulan nanofibers are also suitable for delivery to the large intestine, due to the mucoadhesive properties of the dissolved pullulan.…”

Tandem Repeat of a Short Human Chemerin-Derived Peptide and Its Nontoxic d-Lysine-Containing Enantiomer Display Broad-Spectrum Antimicrobial and Antitubercular Activities

“…Such a palindromic sequence is present in the cathelicidin antimicrobial peptide, tritrpticin . It seems that the palindromic arrangement of amino acids favors interaction with the membrane of pathogens, resulting in the improved antibacterial activity of the corresponding peptide. , …”

“…40 It seems that the palindromic arrangement of amino acids favors interaction with the membrane of pathogens, resulting in the improved antibacterial activity of the corresponding peptide. 41,42 Although amino acids, lysine and arginine, possess the same unit of cationic charge, they show structural differences, particularly in the membrane environment. 43 Thus, the presence of these residues could have impact on the antimicrobial and cytotoxic properties of the corresponding peptide.…”