Cationic Peptide

Iwasaki, Takashi

doi:10.1002/9783527835997.ch4

Cited by 1 publication

(1 citation statement)

References 56 publications

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“…CPPs are about 5-30 residues long, usually linear, (although cyclic versions have been described [27,69]), and mostly composed of L-amino acids, with some sequences including D-residues or L,D-combinations [69]. CPPs have been classified as cationic [175][176][177][178], amphipathic [179][180][181], hydrophobic [182][183][184], or anionic [185,186], with cargoes that include small molecules (drugs and dyes), proteins, nanoparticles, or genetic material [71].…”

Section: Cpp Topoisomers and Drug Delivery Challengesmentioning

confidence: 99%

Topoisomeric Membrane-Active Peptides: A Review of the Last Two Decades

Carrera-Aubesart,

Gallo,

Defaus

et al. 2023

Pharmaceutics

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In recent decades, bioactive peptides have been gaining recognition in various biomedical areas, such as intracellular drug delivery (cell-penetrating peptides, CPPs) or anti-infective action (antimicrobial peptides, AMPs), closely associated to their distinct mode of interaction with biological membranes. Exploiting the interaction of membrane-active peptides with diverse targets (healthy, tumoral, bacterial or parasitic cell membranes) is opening encouraging prospects for peptides in therapeutics. However, ordinary peptides formed by L-amino acids are easily decomposed by proteases in biological fluids. One way to sidestep this limitation is to use topoisomers, namely versions of the peptide made up of D-amino acids in either canonic (enantio) or inverted (retroenantio) sequence. Rearranging peptide sequences in this fashion provides a certain degree of native structure mimicry that, in appropriate contexts, may deliver desirable biological activity while avoiding protease degradation. In this review, we will focus on recent accounts of membrane-active topoisomeric peptides with therapeutic applications as CPP drug delivery vectors, or as antimicrobial and anticancer candidates. We will also discuss the most common modes of interaction of these peptides with their membrane targets.

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