Improving the biological activity of the antimicrobial peptide anoplin by membrane anchoring through a lipophilic amino acid derivative

Slootweg, J. Chris; Schaik, Timo B. van; Ufford, H. C. Quarles van; Breukink, Eefjan; Liskamp, Rob M. J.; Rijkers, Dirk T. S.

doi:10.1016/j.bmcl.2013.05.002

Cited by 27 publications

(19 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The MICs of these bacteria were determined using an established protocol within our group with some minor modifications ( Table 1). 16 The MIC values confirmed our initial expectation that extracellular dual-targeting peptide 1 would prove to be inactive. Peptide 1 caused no inhibition of bacterial growth in all bacterial species tested at high concentration (1mg/mL, 563 µM).…”

supporting

confidence: 73%

Triple-targeting Gram-negative selective antimicrobial peptides capable of disrupting the cell membrane and lipid A biosynthesis

Postma

Liskamp

2016

RSC Adv.

View full text Add to dashboard Cite

supporting

confidence: 73%

Triple-targeting Gram-negative selective antimicrobial peptides capable of disrupting the cell membrane and lipid A biosynthesis

Postma

Liskamp

2016

RSC Adv.

View full text Add to dashboard Cite

“…Hemolysis is commonly used to assess the biosafety of lipopeptides [18,19]. As shown in Fig 3, SLPs have a range hemolytic activities.…”

Section: Hemolytic Activity Of Lipopeptidesmentioning

confidence: 99%

Synthetic surfactin analogues have improved anti-PEDV properties

et al. 2019

View full text Add to dashboard Cite

Surfactin has antiviral activity against various enveloped viruses by inhibiting viral membrane fusion. However, the potential utility of surfactin as an antiviral drug is limited by its cytotoxicity. In this study, 10 surfactin analogues were obtained by chemical synthesis and evaluated to determine their anti-PEDV activities, hemolytic activities, and critical micelle concentrations. The main goal of our study was to develop a safer drug; a surfactin analogue with high anti-PEDV activity and low hemolytic activity. Compared with surfactin, one of the analogues we developed, SLP5, has lower hemolytic activity, with the same antiviral activity. The selectivity index of SLP5 is 52, while the SI for surfactin is 4, in other words, the safe and effective concentration range of SLP5 is 12 times greater than that of surfactin. Like surfactin, SLP5 has a direct antiviral effect on PEDV. Structurally, SLP5 is a linear lipopeptide with three carboxyl groups. Surfactin derivatives similar to SLP5 could be obtained by lactone bond hydrolyzation of surfactin, as well as total synthesis.

show abstract

“…[1,3] Because of their diverse modes of action, a large effort has been made to develop new classes of anti-infective agents based on naturally occurring AMPs. [4–8] …”

Section: Introductionmentioning

confidence: 99%

Improved Bioactivity of Antimicrobial Peptides by Addition of Amino‐Terminal Copper and Nickel (ATCUN) Binding Motifs

2014

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) are promising candidates to help circumvent antibiotic resistance, which is an increasing clinical problem. Amino-terminal copper and nickel (ATCUN) binding motifs are known to actively form reactive oxygen species (ROS) upon metal binding. The combination of these two peptidic constructs could lead to a novel class of dual-acting antimicrobial agents. To test this hypothesis, a set of ATCUN binding motifs were screened for their ability to induce ROS formation, and the most potent were then used to modify AMPs with different modes of action. ATCUN binding motif-containing derivatives of anoplin (GLLKRIKTLL-NH2), pro-apoptotic peptide (PAP; KLAKLAKKLAKLAK-NH2), and sh-buforin (RAGLQFPVGRVHRLLRK-NH2) were synthesized and found to be more active than the parent AMPs against a panel of clinically relevant bacteria. The lower minimum inhibitory concentration (MIC) values for the ATCUN-anoplin peptides are attributed to the higher pore-forming activity along with their ability to cause ROS-induced membrane damage. The addition of the ATCUN motifs to PAP also increases its ability to disrupt membranes. DNA damage is the major contributor to the activity of the ATCUN-sh-buforin peptides. Our findings indicate that the addition of ATCUN motifs to AMPs is a simple strategy that leads to AMPs with higher antibacterial activity and possibly to more potent, usable antibacterial agents.

show abstract

Improving the biological activity of the antimicrobial peptide anoplin by membrane anchoring through a lipophilic amino acid derivative

Cited by 27 publications

References 27 publications

Triple-targeting Gram-negative selective antimicrobial peptides capable of disrupting the cell membrane and lipid A biosynthesis

Triple-targeting Gram-negative selective antimicrobial peptides capable of disrupting the cell membrane and lipid A biosynthesis

Synthetic surfactin analogues have improved anti-PEDV properties

Improved Bioactivity of Antimicrobial Peptides by Addition of Amino‐Terminal Copper and Nickel (ATCUN) Binding Motifs

Contact Info

Product

Resources

About