Results 11 to 20 of about 53,767 (297)
Antimicrobial peptide-inspired antibacterial polymeric materials for biosafety
Biosafety and Health, 2022 The emergence of antimicrobial resistance attributed to the overuse and abuse of antibiotics severely endangers global biosafety. Antimicrobial peptides (AMPs) produced by various living organisms exhibit broad-spectrum antimicrobial properties with a ...
Min Lin, Jing Sun
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Microbiology Spectrum, 2022 Bacterial efflux pumps in the resistance-nodulation-cell division (RND) family of Gram-negative bacteria contribute significantly to the development of antimicrobial resistance by many pathogens. In this study, we selected the MtrD transporter protein of
Meinan Lyu +5 more
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Cationic Antimicrobial Peptide Cytotoxicity [PDF]
SOJ Microbiology & Infectious Diseases, 2014 Fluorescence microscopy serves as a valuable tool for assessing the structural integrity and viability of eukaryotic cells. Through the use of calcein AM and the DNA stain 4,6-diamidino-2 phenylindole (DAPI), cell viability and membrane integrity can be qualified. Our group has previously shown the ultra-short cationic antimicrobial peptide H-OOWW-NH2;
Laverty, Garry, Gilmore, Brendan
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Cationic Hydrophobic Peptides with Antimicrobial Activity [PDF]
Antimicrobial Agents and Chemotherapy, 2002 ABSTRACT The MICs of cationic, hydrophobic peptides of the prototypic sequence KKAAAXAAAAAXAAWAAXAAAKKKK-amide (where X is one of the 20 commonly occurring amino acids) are in a low micromolar range for a panel of gram-negative and gram-positive bacteria, with no or low hemolytic activity against human and rabbit erythrocytes.
Margareta, Stark +2 more
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The frog skin-derived antimicrobial peptide esculentin-1a(1-21)nh2 promotes the migration of human hacat keratinocytes in an egf receptor-dependent manner: a novel promoter of human skin wound healing? [PDF]
, 2015 One of the many functions of skin is to protect the organism against a wide range of pathogens. Antimicrobial peptides (AMPs) produced by the skin epithelium provide an effective chemical shield against microbial pathogens. However, whereas antibacterial/
Cappiello, Floriana +6 more
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Chain-end modifications and sequence arrangements of antimicrobial peptoids for mediating activity and nano-assembly [PDF]
, 2020 Poly(N-substituted glycine) “peptoids” are an interesting class of peptidomimics that can resist proteolysis and mimic naturally found antimicrobial peptides (AMPs), which exhibit wide spectrum activity against bacteria.
Castelletto, Valeria +9 more
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Characterization of the Hemolytic Activity of Mastoparan Family Peptides from Wasp Venoms
Toxins, 2023 Biologically active peptides have attracted increasing attention in research on the development of new drugs. Mastoparans, a group of wasp venom linear cationic α-helical peptides, have a variety of biological effects, including mast cell degranulation ...
Xiangdong Ye +10 more
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Salt-Resistant Alpha-Helical Cationic Antimicrobial Peptides [PDF]
Antimicrobial Agents and Chemotherapy, 1999 ABSTRACT Analogues based on the insect cecropin–bee melittin hybrid peptide (CEME) were studied and analyzed for activity and salt resistance. The new variants were designed to have an increase in amphipathic α-helical content (CP29 and CP26) and in overall positive charge (CP26). The α-helicity of these peptides was demonstrated
C, Friedrich +4 more
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Short Cationic Antimicrobial Peptides Interact with ATP [PDF]
Antimicrobial Agents and Chemotherapy, 2010 ABSTRACT The mode of action of short, nonhelical antimicrobial peptides is still not well understood. Here we show that these peptides interact with ATP and directly inhibit the actions of certain ATP-dependent enzymes, such as firefly luciferase, DnaK, and DNA polymerase.
Hilpert, K. +10 more
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Synthesis and cellular penetration properties of new phosphonium based cationic amphiphilic peptides [PDF]
, 2018 A new category of phosphonium based cationic amphiphilic peptides has been developed and evaluated as potential antimicrobial peptides and cell penetrating peptides.
Gannon, Susan +7 more
core +1 more source