Piscidin-1-analogs with double L- and D-lysine residues exhibited different conformations in lipopolysaccharide but comparable anti-endotoxin activities

相似書籍

• Single Amino Acid Substitutions at Specific Positions of the Heptad Repeat Sequence of Piscidin-1 Yielded Novel Analogs That Show Low Cytotoxicity and In Vitro and In Vivo Antiendotoxin Activity
  由: Kumar, Amit, et al.
  出版: (2016)
• Cell-Selective Pore Forming Antimicrobial Peptides of the Prodomain of Human Furin: A Conserved Aromatic/Cationic Sequence Mapping, Membrane Disruption, and Atomic-Resolution Structure and Dynamics
  由: Sheetal Sinha, et al.
  出版: (2018-11-01)
• Cell-Selective Pore Forming Antimicrobial Peptides of the Prodomain of Human Furin: A Conserved Aromatic/Cationic Sequence Mapping, Membrane Disruption, and Atomic-Resolution Structure and Dynamics
  由: Sinha, Sheetal, et al.
  出版: (2018)
• Identification of GXXXXG motif in Chrysophsin-1 and its implication in the design of analogs with cell-selective antimicrobial and anti-endotoxin activities
  由: Tripathi, Amit Kumar, et al.
  出版: (2017)
• A TLR4-derived non-cytotoxic, self-assembling peptide functions as a vaccine adjuvant in mice
  由: Tandon, Anshika, et al.
  出版: (2018)