Design of imperfectly amphipathic α-helical antimicrobial peptides with enhanced cell selectivity

X Zhu, N Dong, Z Wang, Z Ma, L Zhang, Q Ma, A Shan - Acta biomaterialia, 2014 - Elsevier
Antimicrobial peptides (AMPs), which are produced by multicellular organisms as a defense
mechanism against competing pathogenic microbes, appear to be excellent candidates for …

The effect of acidic residues and amphipathicity on the lytic activities of mastoparan peptides studied by fluorescence and CD spectroscopy

NB Leite, LC Da Costa, D dos Santos Alvares… - Amino Acids, 2011 - Springer
Some mastoparan peptides extracted from social wasps display antimicrobial activity and
some are hemolytic and cytotoxic. Although the cell specificity of these peptides is complex …

Design, synthesis, and nanostructure-dependent antibacterial activity of cationic peptide amphiphiles

N Rodrigues de Almeida, Y Han, J Perez… - … applied materials & …, 2018 - ACS Publications
The development of bacterial resistant strains is a global health concern. Designing
antibiotics that limit the rise of pathogenic resistance is essential to efficiently treat …

Hydrophobic-hydrophilic alternation: an effective pattern to de novo designed antimicrobial peptides

Q Cheng, P Zeng - Current Pharmaceutical Design, 2022 - ingentaconnect.com
The antimicrobial peptide (AMP) is a class of molecules that are active against a variety of
microorganisms, from bacterial and cancer cells to fungi. Most AMPs are natural products, as …

Probing Mastoparan-like Antimicrobial Peptides Interaction with Model Membrane Through Energy Landscape Analysis

IBS Martins, RG Viegas, MN Sanches… - The Journal of …, 2023 - ACS Publications
Antimicrobial Peptides (AMPs) have emerged as promising alternatives to conventional
antibiotics due to their capacity to disrupt the lipid packing of bacterial cell membranes. This …

Morphing of amphipathic helices to explore the activity and selectivity of membranolytic antimicrobial peptides

AT Müller, G Posselt, G Gabernet, C Neuhaus… - Biochemistry, 2020 - ACS Publications
Naturally occurring membranolytic antimicrobial peptides (AMPs) are rarely cell-type
selective and highly potent at the same time. Template-based peptide design can be used to …

Selectivity in the mechanism of action of antimicrobial mastoparan peptide Polybia-MP1

MP dos Santos Cabrera, STB Costa… - European Biophysics …, 2008 - Springer
Many potent antimicrobial peptides also present hemolytic activity, an undesired collateral
effect for the therapeutic application. Unlike other mastoparan peptides, Polybia-MP1 …

Manipulating active structure and function of cationic antimicrobial peptide CM15 with the polysulfonated drug suramin: a step closer to in vivo complexity

M Quemé‐Peña, T Juhász, J Mihály… - …, 2019 - Wiley Online Library
Antimicrobial peptides (AMPs) kill bacteria by targeting their membranes through various
mechanisms involving peptide assembly, often coupled with disorder‐to‐order structural …

Insights into the antimicrobial activity and cytotoxicity of engineered α-helical peptide amphiphiles

Z Ma, J Yang, J Han, L Gao, H Liu, Z Lu… - Journal of Medicinal …, 2016 - ACS Publications
Antimicrobial peptides (AMPs) have gained increasing attention, as they can overcome
recurring microbial invasions. However, their poor antimicrobial activity and potential …

Influence of chain length on the anticancer activity of the antimicrobial peptide CAMEL with fatty acid modification

L Ma, S Huang, H Xie, P Ma, B Jia, Y Yao, Y Gao… - European Journal of …, 2022 - Elsevier
Antimicrobial peptides (AMPs) display promising potential in cancer therapy. Modification
with fatty acids is a simple and effective approach to improve the activity of AMPs. In the …