Interaction between amphiphilic peptides and phospholipid membranes
TLDR
This brief review aims at providing some illustrative examples on the interaction between amphiphilic peptides and phospholipid membranes an area of significant current interest focusing on antimicrobial peptides.Abstract:
This brief review aims at providing some illustrative examples on the interaction between amphiphilic peptides and phospholipid membranes an area of significant current interest Focusing on antimicrobial peptides factors affecting peptide-membrane interactions are addressed including effects of peptide length charge hydrophobicity secondary structure and topology Effects of membrane composition are also illustrated including effects of membrane charge nature of the polar headgroup and presence of cholesterol and other sterols Throughout novel insights on the importance of peptide adsorption density on membrane stability are emphasized as is the correlation between peptide adsorption peptide induced leakage in model liposome systems peptide-induced lysis of bacteria and bacteria killing (C) 2010 Elsevier Ltd All rights reserved (Less)read more
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A pH-responsive α-helical cell penetrating peptide-mediated liposomal delivery system.
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Antimicrobial and antiviral hydrogels
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References
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Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
TL;DR: In this review the different models of antimicrobial-peptide-induced pore formation and cell killing are presented and several observations suggest that translocated peptides can alter cytoplasmic membrane septum formation, inhibit cell-wall synthesis, inhibit nucleic-acid synthesis, inhibits protein synthesis or inhibit enzymatic activity.
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Amphipathic, α‐helical antimicrobial peptides
TL;DR: This review considers alpha-helical, antimicrobial peptides from the point of view of six interrelated structural and physicochemical parameters that modulate their activity and specificity: sequence, size, structuring, charge, amphipathicity, and hydrophobicity.
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LL-37, the only human member of the cathelicidin family of antimicrobial peptides.
TL;DR: LL-37, the only cathelicidin-derived antimicrobial peptide found in humans, is shown to exhibit a broad spectrum of antimicrobial activity and has been found to have additional defensive roles such as regulating the inflammatory response and chemo-attracting cells of the adaptive immune system to wound or infection sites.