Improved Cell Selectivity of Symmetric α‐Helical Peptides Derived From Trp‐Rich Antimicrobial Peptides

2020 ◽  
Vol 41 (9) ◽  
pp. 930-936
Author(s):  
Hyunhee Lee ◽  
Sungtae Yang ◽  
Song Yub Shin
Keyword(s):  
Antimicrobial Peptides ◽  
Helical Peptides ◽  
Cell Selectivity

scholarly journals Design of Embedded-Hybrid Antimicrobial Peptides with Enhanced Cell Selectivity and Anti-Biofilm Activity

PLoS ONE ◽  
2014 ◽  
Vol 9 (6) ◽  
pp. e98935 ◽  
Author(s):  
Wei Xu ◽  
Xin Zhu ◽  
Tingting Tan ◽  
Weizhong Li ◽  
Anshan Shan
Keyword(s):  
Antimicrobial Peptides ◽  
Cell Selectivity

scholarly journals Effect of helical kink in antimicrobial peptides on membrane pore formation

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Alzbeta Tuerkova ◽  
Ivo Kabelka ◽  
Tereza Králová ◽  
Lukáš Sukeník ◽  
Šárka Pokorná ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Pore Formation ◽  
Molecular Level ◽  
Helical Peptides ◽  
Membrane Pore ◽  
Bacterial Membranes ◽  
Membrane Pores ◽  
Helical Peptide ◽  
Toroidal Pore ◽  
The Right

Every cell is protected by a semipermeable membrane. Peptides with the right properties, for example Antimicrobial peptides (AMPs), can disrupt this protective barrier by formation of leaky pores. Unfortunately, matching peptide properties with their ability to selectively form pores in bacterial membranes remains elusive. In particular, the proline/glycine kink in helical peptides was reported to both increase and decrease antimicrobial activity. We used computer simulations and fluorescence experiments to show that a kink in helices affects the formation of membrane pores by stabilizing toroidal pores but disrupting barrel-stave pores. The position of the proline/glycine kink in the sequence further controls the specific structure of toroidal pore. Moreover, we demonstrate that two helical peptides can form a kink-like connection with similar behavior as one long helical peptide with a kink. The provided molecular-level insight can be utilized for design and modification of pore-forming antibacterial peptides or toxins.

How Cell Concentrations Are Implicated in Cell Selectivity of Antimicrobial Peptides

Langmuir ◽  
2015 ◽  
Vol 31 (29) ◽  
pp. 8052-8062 ◽  
Author(s):  
Azadeh Bagheri ◽  
Sattar Taheri-Araghi ◽  
Bae-Yeun Ha
Keyword(s):  
Antimicrobial Peptides ◽  
Cell Selectivity ◽  
Cell Concentrations

Central β-turn increases the cell selectivity of imperfectly amphipathic α-helical peptides

2018 ◽  
Vol 69 ◽  
pp. 243-255 ◽  
Author(s):  
Changxuan Shao ◽  
Haotian Tian ◽  
Tianyu Wang ◽  
Zhihua Wang ◽  
Shuli Chou ◽  
...  
Keyword(s):  
Helical Peptides ◽  
Cell Selectivity

scholarly journals Effect of Helical Kink in Antimicrobial Peptides on Membrane Pore Formation

2019 ◽  
Author(s):  
Alzbeta Tuerkova ◽  
Ivo Kabelka ◽  
Tereza Králová ◽  
Lukáš Sukeník ◽  
Šárka Pokorná ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Pore Formation ◽  
Molecular Level ◽  
Helical Peptides ◽  
Membrane Pore ◽  
Bacterial Membranes ◽  
Membrane Pores ◽  
Helical Peptide ◽  
Toroidal Pore ◽  
The Right

AbstractEvery cell is protected by a semipermeable membrane. Peptides with the right properties, e.g. Antimicrobial peptides (AMPs), can disrupt this protective barrier by formation of leaky pores. Unfortunately, matching peptide properties with their ability to selectively form pores in bacterial membranes remains elusive. In particular, the proline/glycine kink in helical peptides was reported to both increase and decrease antimicrobial activity. We used computer simulations and fluorescence experiments to show that a kink in helices affects the formation of membrane pores by stabilizing toroidal pores but disrupting barrel-stave pores. The position of the proline/glycine kink in the sequence further controls the specific structure of toroidal pore. Moreover, we demonstrate that two helical peptides can form a kink-like connection with similar behavior as one long helical peptide with a kink. The provided molecular-level insight can be utilized for design and modification of pore forming antibacterial peptides or toxins.

Cell-selectivity of tryptophan and tyrosine in amphiphilic α-helical antimicrobial peptides against drug-resistant bacteria

2018 ◽  
Vol 505 (2) ◽  
pp. 478-484 ◽  
Author(s):  
Min-Young Lee ◽  
Seong-Cheol Park ◽  
Myunghwan Jung ◽  
Min-Kyoung Shin ◽  
Hyung-Lyun Kang ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Resistant Bacteria ◽  
Drug Resistant ◽  
Cell Selectivity ◽  
Drug Resistant Bacteria

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

2014 ◽  
Vol 10 (1) ◽  
pp. 244-257 ◽  
Author(s):  
Xin Zhu ◽  
Na Dong ◽  
Zeyun Wang ◽  
Zhi Ma ◽  
Licong Zhang ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Cell Selectivity
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