Peptides that exert antimicrobial activity in artificial media may lack activity within blood or other complex biological matrices. To facilitate the evaluation of antimicrobial peptides for possible therapeutic utility, an ex vivo assay was developed to assess the extent and durability of peptide antimicrobial activities in complex fluid biomatrices of whole blood, plasma, and serum compared w...

Antimicrobial peptides (AMPs) possess bactericidal activity against a variety of pathogens depending on an overall balance positively charged and hydrophobic residues. Selective fluorination serves to fine-tune the intrinsic hydrophobicity that could improve AMP bioactivity without affecting sequence length. Only few studies have focused impact this unique element antimicrobial potency came som...

Antimicrobial peptides are a class of small, usually positively charged amphiphilic peptides that are used by the innate immune system to combat bacterial infection in multicellular eukaryotes. Antimicrobial peptides are known for their broad-spectrum antimicrobial activity and thus can be used as a basis for a development of new antibiotics against multidrug-resistant bacteria. The most challe...

The protegrin family of antimicrobial peptides is among the shortest in sequence length while remaining very active against a variety of microorganisms. The major goal of this study is to characterize easily calculated molecular properties, which quantitatively show high correlation with antibacterial activity. The peptides studied have high sequence similarity but vary in activity over more th...

BACKGROUND Antimicrobial peptides (AMPs) are receiving increasing attention due to resistance development against conventional antibiotics. Pseudomonas aeruginosa and Staphylococcus aureus are two major pathogens involved in an array of infections such as ocular infections, cystic fibrosis, wound and post-surgery infections, and sepsis. The goal of the study was to design novel AMPs against the...

The phenomenon of antimicrobial resistance threatens our ability to treat common infections. clinical pipeline for new antimicrobials is pretty much dry and hence, there a need the development agents with low toxicities help fight resistant microorganisms. This work aimed design peptides using database filtering technology evaluate their bioactivities. physicochemical properties designed were e...

Over the past decade, levels of bacterial resistance to antibiotics have risen dramatically and "superbugs" resistant to most or all available agents have appeared in the clinic. Thus there is a growing need to discover and introduce new drugs. One potential source of novel antibiotics is the cationic antimicrobial peptides, which have been isolated from most living entities as components of th...

Halocidin is a heterodimer antimicrobial peptide previously isolated from the tunicate Halocynthia aurantium. Based on the larger monomer (18Hc) of halocidin, nine halocidin congeners, including a series of 6 peptides truncated successively from the carboxyl-terminal end of 18Hc and 3 analogs (18HcKK, K19Hc, and K19HcKK), which have lysine residues in place of two internal histidines or have a ...

Antimicrobial peptides (AMPs) have recently become widely publicized because they the potential to function in alternative therapies as “natural” antibiotics, with their main advantage being a broad spectrum of activity. The for antimicrobial treat diabetes mellitus (DM) has been reported. In type I (T1D), cathelicidin-related peptide (CRAMP), cathelicidin (CAMP) and mouse-β- defensin 14 (mBD14...

The preclinical in vitro and in vivo benchmark figures of cationic antimicrobial peptides have to be revisited based on the newly discovered alternative modes of action.