Balancing hydrophobicity and sequence pattern to influence self‐assembly of amphipathic peptides
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DOI: 10.1002/bip.23099
Abstract: Amphipathic peptides with alternating polar and nonpolar amino acid sequences efficiently self‐assemble into functional β‐sheet fibrils as long as the nonpolar residues have sufficient hydrophobicity. For example, the Ac‐(FKFE)2‐NH2 peptide rapidly self‐assembles into β‐sheet bilayer… read more here.
Keywords: self assembly; hydrophobicity; phe; amphipathic peptides ... See more keywords
Phenol‐Soluble‐Modulin‐Inspired Amphipathic Peptides Have Bactericidal Activity against Multidrug‐Resistant Bacteria
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DOI: 10.1002/cmdc.201900364
Abstract: Phenol‐soluble modulins (PSMs) are a large family of cytolytic peptide toxins produced by Staphylococcus aureus. Based on their amino acid sequences, we have constructed a small library of cationic isoleucine‐rich peptides for antimicrobial evaluation. Relative… read more here.
Keywords: inspired amphipathic; phenol soluble; amphipathic peptides; modulin inspired ... See more keywords
Synthesis and Application of Peptide-siRNA Nanoparticles from Disulfide-Constrained Cyclic Amphipathic Peptides for the Functional Delivery of Therapeutic Oligonucleotides to the Lung.
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DOI: 10.1007/978-1-0716-0928-6_4
Abstract: The potential of RNAi therapies has been largely impeded by the inherent challenges in the functional delivery of siRNA to cells. Herein, we describe protocols for the synthesis and characterization of novel peptide-siRNA nanoparticles prepared… read more here.
Keywords: disulfide constrained; delivery; peptide sirna; functional delivery ... See more keywords