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

• Main Authors: Kumar, Amit, Mahajan, Mukesh, Awasthi, Bhanupriya, Tandon, Anshika, Harioudh, Munesh Kumar, Shree, Sonal, Singh, Pratiksha, Shukla, Praveen Kumar, Ramachandran, Ravishankar, Mitra, Kalyan, Bhattacharjya, Surajit, Ghosh, Jimut Kanti
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2017
• Subjects: Inflammation; Peptides
• Online Access: https://hdl.handle.net/10356/83571; http://hdl.handle.net/10220/42671
• Institution: Nanyang Technological University

To become clinically effective, antimicrobial peptides (AMPs) should be non-cytotoxic to host cells. Piscidins are a group of fish-derived AMPs with potent antimicrobial and antiendotoxin activities but limited by extreme cytotoxicity. We conjectured that introduction of cationic residue(s) at the i...