Cell selectivity and mechanism of action of short antimicrobial peptides designed from the cell-penetrating peptide Pep-1

2009 ◽  
Vol 15 (9) ◽  
pp. 569-575 ◽  
Author(s):  
Wan Long Zhu ◽  
Kyung-Soo Hahm ◽  
Song Yub Shin
Keyword(s):  
Antimicrobial Peptides ◽  
Mechanism Of Action ◽  
Cell Penetrating Peptide ◽  
Cell Selectivity ◽  
Cell Penetrating

Structure optimisation to improve the delivery efficiency and cell selectivity of a tumour-targeting cell-penetrating peptide

2018 ◽  
Vol 26 (9) ◽  
pp. 777-792 ◽  
Author(s):  
Xue-Wei Cao ◽  
Xu-Zhong Yang ◽  
Xuan Du ◽  
Long-Yun Fu ◽  
Tao-Zhu Zhang ◽  
...  
Keyword(s):  
Cell Penetrating Peptide ◽  
Tumour Targeting ◽  
Cell Selectivity ◽  
Cell Penetrating ◽  
Delivery Efficiency

scholarly journals Bacterial Spheroplasts as a Model for Visualizing Membrane Translocation of Antimicrobial Peptides

2016 ◽  
Vol 60 (10) ◽  
pp. 6350-6352 ◽  
Author(s):  
Lei Wei ◽  
Maria A. LaBouyer ◽  
Louise E. O. Darling ◽  
Donald E. Elmore
Keyword(s):  
Antimicrobial Peptides ◽  
Light Microscopy ◽  
Mechanism Of Action ◽  
Cell Penetrating Peptides ◽  
Bacterial Cells ◽  
Membrane Translocation ◽  
Cell Penetrating ◽  
Localization Data ◽  
Conventional Light Microscopy

ABSTRACTStudies attempting to characterize the membrane translocation of antimicrobial and cell-penetrating peptides are frequently limited by the resolution of conventional light microscopy. This study shows that spheroplasts provide a valuable approach to overcome these limits. Spheroplasts produce less ambiguous images and allow for more systematic analyses of localization. Data collected with spheroplasts are consistent with studies using normal bacterial cells and imply that a particular peptide may not always follow the same mechanism of action.

scholarly journals Characterization of the antimicrobial activity of the cell-penetrating peptide TAT-RasGAP317-326

2020 ◽  
Author(s):  
Maria Georgieva ◽  
Tytti Heinonen ◽  
Alessandra Vitale ◽  
Simone Hargraves ◽  
Senka Causevic ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Bacterial Resistance ◽  
Divalent Cations ◽  
Low Ph ◽  
Resistant Bacteria ◽  
Cell Penetrating Peptide ◽  
Cell Penetrating ◽  
Emergence Of Resistance ◽  
Insight Into

AbstractThe efficiency of classical antibiotics is undermined by the emergence of resistance. Antimicrobial peptides (AMPs) may represent an alternative to antibiotics currently used in the clinic. TAT-RasGAP317-326 is one of such AMP. It is a cell-penetrating peptide with broad antimicrobial activity against Gram-positive and Gram-negative bacteria. However, the mechanisms allowing this peptide to kill bacteria are not characterized. Here, we aim to provide a better understanding of the factors influencing TAT-RasGAP317-326 antimicrobial activity.In this article, we show that divalent cations, serum proteins, and low pH levels modulate TAT-RasGAP317-326 activity against bacteria. We demonstrate that low pH and divalent cations reduce the binding of the peptide to bacteria. Using transcriptomics and screening of bacterial mutant libraries, we mapped the transcriptional response of TAT-RasGAP317-326-exposed bacteria and highlighted cellular pathways that may play a role in bacterial resistance to this peptide. We tested combinations of TAT-RasGAP317-326 with other AMPs and detected an inhibitory effect of melittin on TAT-RasGAP317-326 activity. Finally, we performed a resistance selection screen that revealed differences between bacterial strains with respect to their rate of resistance emergence against TAT-RasGAP317-326.Our study provides the first investigation of factors that impact the antimicrobial activity of TAT-RasGAP317-326 and brings insights into the mechanisms underlying the peptide’s activity.ImportanceAntibiotic resistance is an increasing concern for modern medicine. Resistant bacteria cause life-threatening infections that are very challenging to treat. Antimicrobial peptides (AMPs) could be a promising alternative to classical antibiotics because of their antibacterial properties and low propensity for the development of bacterial resistance. To maximize the efficiency of AMPs and avoid the emergence of resistance, it is important to understand the factors affecting their activity. In this study, we investigate the antimicrobial activity of a recently described AMP, TAT-RasGAP317-326. We outline a subset of extracellular factors that influence its antimicrobial activity and characterize the bacterial response to this AMP. Our findings here also provide vital insight into the potential of bacteria developing resistance to this TAT-RasGAP317-326 peptide. Overall, this study provides important insight into the basic mechanism of action of TAT-RasGAP317-326 and a better understanding of the interaction between TAT-RasGAP317-326 and its bacterial targets.

scholarly journals Designed Cell-Penetrating Peptide Inhibitors of Amyloid-beta Aggregation and Cytotoxicity

2020 ◽  
Vol 1 (2) ◽  
pp. 100014 ◽  
Author(s):  
Anja Henning-Knechtel ◽  
Sunil Kumar ◽  
Cecilia Wallin ◽  
Sylwia Król ◽  
Sebastian K.T.S. Wärmländer ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
Peptide Inhibitors ◽  
Cell Penetrating Peptide ◽  
Cell Penetrating

18F-Labeled phosphopeptide-cell-penetrating peptide dimers with enhanced cell uptake properties in human cancer cells

2012 ◽  
Vol 39 (8) ◽  
pp. 1202-1212 ◽  
Author(s):  
Susan Richter ◽  
Vincent Bouvet ◽  
Melinda Wuest ◽  
Ralf Bergmann ◽  
Joerg Steinbach ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Human Cancer ◽  
Cell Uptake ◽  
Cell Penetrating Peptide ◽  
Human Cancer Cells ◽  
Cell Penetrating
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