2022
DOI: 10.1515/epoly-2022-0012
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Study on the self-assembly of aromatic antimicrobial peptides based on different PAF26 peptide sequences

Abstract: Antimicrobial peptide (AMP) self-assembly is an effective way to synthesis antimicrobial biomaterials. In previous studies, we found PAF26 AMP (Ac-RKKWFW-NH2) and its derivative K2–F2 peptide (Ac-KKRKKWFWFF-NH2) could both self-assemble into hydrogels, but they had distinct microscopic structures. Therefore, in this work five PAF26 peptide derivatives with different numbers of aromatic amino acids are designed to better understand the self-assembly mechanism of aromatic AMP. The transmission electron microscop… Show more

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Cited by 7 publications
(4 citation statements)
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“…(2) Ionic complementary peptides (e.g., EAR16-II, EAR8-II, EAR8-IIa, and ELR8-IIa) which are charactered by regular distribution of charged amino acid residues. 17 The oppositely charged amino acid residues provide electrostatic attractive interactions, leading to fibrilization: (3) aromatic peptides containing F, W, and Y, such as KRW6, KRW6-F, KRW6-FF, KKRW6, and KKRW6-F. 18 Fibrilization of aromatic peptides is driven by π−π stacking between aromatic rings as well as hydrogen bonds. The pH affects peptide self-assembly by modulating hydrophobic and electrostatic interactions.…”
Section: ■ Introductionmentioning
confidence: 99%
“…(2) Ionic complementary peptides (e.g., EAR16-II, EAR8-II, EAR8-IIa, and ELR8-IIa) which are charactered by regular distribution of charged amino acid residues. 17 The oppositely charged amino acid residues provide electrostatic attractive interactions, leading to fibrilization: (3) aromatic peptides containing F, W, and Y, such as KRW6, KRW6-F, KRW6-FF, KKRW6, and KKRW6-F. 18 Fibrilization of aromatic peptides is driven by π−π stacking between aromatic rings as well as hydrogen bonds. The pH affects peptide self-assembly by modulating hydrophobic and electrostatic interactions.…”
Section: ■ Introductionmentioning
confidence: 99%
“…The cooperative action of hydrogen bonding, hydrophobic interaction, and electrostatic attraction drive the formation of self-assembled nanostructures of AMPs; properties such as hydrophobicity, aromaticity, geometry, charge, and isoelectric point of various amino acid residues determine AMPs' secondary structures, allowing the formation of self-assembled nanostructures by carefully engineering amino acids sequences in synthetic AMPs [17,20,22,23].…”
Section: Introducing Antimicrobial Peptides In Pharmacologymentioning
confidence: 99%
“…Nanotechnology has also been providing promising approaches for formulating and delivering AMPs [22,[36][37][38][39]. AMPs can be protected by nanostructures, having their low stability circumvented and their release controlled by appropriate pharmacodynamics; thereby, antimicrobial activity, retention, and biosafety could be enhanced [40,41].…”
Section: Introducing Antimicrobial Peptides In Pharmacologymentioning
confidence: 99%
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