We used a template-assisted approach to develop synthetic antimicrobial peptides, which
differ from naturally occurring antimicrobial peptides that can compromise host natural …

A major barrier to the use of antimicrobial peptides as antibiotics is the toxicity or ability to
lyse eukaryotic cells. In this study, a 26-residue amphipathic α-helical antimicrobial peptide …

In the present study, the 26-residue peptide sequence Ac-
KWKSFLKTFKSAVKTVLHTALKAISS-amide (V 681) was utilized as the framework to study …

A series of 12‐amino acid peptide analogs is designed using point mutation strategy based
on an α‐helical peptide template. The first mutation in the series, KL12, has an idealized …

In the present study, the 26-residue peptide sequence Ac-
KWKSFLKTFKSAKKTVLHTALKAISS-amide (peptide P) was utilized as the framework to …

As potential therapeutic agents, antimicrobial peptides with shorter length and simpler
amino acid composition can be better candidates for clinical and commercial development …

Antimicrobial peptides (AMPs) are excellent candidates to combat the increasing number of
multi-or pan-resistant pathogens worldwide based on their mechanism of action, which is …

A series of small (7–12 mer) amphipathic cationic peptides were designed and synthesized
to create short helical peptides with broad-range bactericidal activity and selectivity toward …

The emergence of multidrug-resistant (MDR) pathogens underscores the need for new
antimicrobial agents to overcome the resistance mechanisms of these organisms. Cationic …

De novo design of amphipathic model peptides has been successful for generating many
antimicrobial peptides with various lengths and amino acid compositions. Here, we suggest …