Control of cell selectivity of antimicrobial peptides.

By K. Matsuzaki. Biochimica et Biophysica Acta, 2009

662 citations recorded by the source corpus.

Antimicrobial peptides (AMPs) are promising novel antibiotics, because they exhibit broad antimicrobial spectra and do not easily induce resistance. For clinical applications, it is important to develop potent AMPs with less toxicity against host cells. This review article summarizes the molecular basis for the cell selectivity (bacteria versus host cells) of AMPs and various attempts to control it, including the optimization of physicochemical parameters of peptides, the introduction of D-, fluorinated, and unusual amino acids into peptides, the constraining of peptide conformations, and the modification of peptides by polymers. Pros and cons of these approaches are discussed.

Subfields: Microbiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/44727696087842119d100fa72b86865f2ec6afb8

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Citations in the corpus

Antimicrobial Peptides: An Emerging Category of Therapeutic Agents (2016, background): “Notably, bacterial cells typically have an inside-negative transmembrane potential between −130 and −150 mV in contrast to mammalian cells, where the potential ranges from −90 to −110 mV (Yeaman and Yount, 2003; Matsuzaki, 2009; Ebenhan et al., 2014).”
Designing antimicrobial peptides: form follows function (2011, background): “In many cases these design principles are analogous to those described above and will benefit from prior experiences in this arena with natural peptides 176,177 .”
Antimicrobial Peptides (2013, background): “Despite these advantageous features of AMPs, there are still some challenges to their applications, such as potential toxicity to humans [12,55,56], sensitivity to harsh environmental conditions (susceptibility to proteases and extreme pH [57,58]), lack of selectivity against specific strains [59], ”
Peptides: A Package for Data Mining of Antimicrobial Peptides (2015, background): “Multiple research have concluded that the natural biological activities of these peptides are coordinated by a sophisticated modulation of the hydrophobicity, amphipathicity, positive charge and a reduction in the hydrophobic moment (Yeaman and Yount, 2003; Fjell et al., 2012; Matsuzaki, 2009).”