Chemically modified and conjugated antimicrobial peptides against superbugs

W Li, F Separovic, NM O'Brien-Simpson… - Chemical Society …, 2021 - pubs.rsc.org
Antimicrobial resistance (AMR) is one of the greatest threats to human health that, by 2050,
will lead to more deaths from bacterial infections than cancer. New antimicrobial agents …

Dimerization of antimicrobial peptides: a promising strategy to enhance antimicrobial peptide activity

EN Lorenzon, JP Piccoli… - Protein and peptide …, 2019 - ingentaconnect.com
Antimicrobial resistance is a global health problem with strong social and economic impacts.
The development of new antimicrobial agents is considered an urgent challenge. In this …

Biomaterial‐interrelated bacterial sweeper: simplified self‐assembled octapeptides with double‐layered Trp zipper induces membrane destabilization and bacterial …

Y Fang, Y Zhu, L Li, Z Lai, N Dong, A Shan - Small Methods, 2021 - Wiley Online Library
Abstract Treatment of microbial‐associated infections continues to be hampered by impaired
antibacterial efficiency and the variability in nanomedicines. Herein, an octapeptide library …

Effect of an antimicrobial peptide on lateral segregation of lipids: a structure and dynamics study by neutron scattering

VK Sharma, S Qian - Langmuir, 2019 - ACS Publications
Antimicrobial peptides are one of the most promising classes of antibiotic agents for drug-
resistant bacteria. Although the mechanisms of their action are not fully understood, many of …

A critical review of short antimicrobial peptides from scorpion venoms, their physicochemical attributes, and potential for the development of new drugs

PA Fong-Coronado, V Ramirez… - The Journal of …, 2024 - Springer
Scorpion venoms have proven to be excellent sources of antimicrobial agents. However,
although many of them have been functionally characterized, they remain underutilized as …

Interaction of the antimicrobial peptide aurein 1.2 and charged lipid bilayer

DK Rai, S Qian - Scientific reports, 2017 - nature.com
Aurein 1.2 is a potent antimicrobial peptide secreted by frog Litoria aurea. As a short
membrane-active peptide with only 13 amino acids in sequence, it has been found to be …

Interaction of a short antimicrobial peptide on charged lipid bilayer: A case study on aurein 1.2 peptide

S Qian, PA Zolnierczuk - BBA advances, 2022 - Elsevier
Abstract Aurein 1.2 (aurein) is a short but active α-helical antimicrobial peptide discovered in
Australian tree frogs (Litoria aurea). It shows inhibition on a broad spectrum of bacteria and …

Understanding the mechanism of action of peptide (p-BthTX-I) 2 derived from C-terminal region of phospholipase A2 (PLA2)-like bothropstoxin-I on Gram-positive and …

NA Santos-Filho, LM de Freitas, CT Dos Santos… - Toxicon, 2021 - Elsevier
Based on the antimicrobial activity of bothropstoxin-I (BthTX-I) and on the premise that a C-
terminal peptide of Lys49 myotoxin can reproduce the antimicrobial activity of the parent …

Interaction of cationic antimicrobial peptides from Australian frogs with lipid membranes

S Zhu, MA Sani, F Separovic - Peptide Science, 2018 - Wiley Online Library
Cationic antimicrobial peptides (AMPs) from Australian frogs have been extensively studied
as alternatives to traditional antibiotics. Solid‐state NMR is used to characterize their effect …

Antimicrobial activity and mechanism of action of a novel peptide present in the ecdysis process of centipede Scolopendra subspinipes subspinipes

E Chaparro-Aguirre, PJ Segura-Ramírez, FL Alves… - Scientific Reports, 2019 - nature.com
One of the most important cellular events in arthropods is the moulting of the cuticle
(ecdysis). This process allows them to grow until they reach sexual maturity. Nevertheless …