Nmr Structural Studies of Antimicrobial Peptides, LPcin

Abstract

1Z profiles followed a theoretical square-law functional dependence [4]. Our preliminary results show that R 2 CP is sensitive to hydration levels as well as the acyl position, thus indicating the presence of slow dynamic modes. The R 2 CP rates of the acyl segments near the polar head groups increase with lipid dehydration, while the acyl segments deeper in the hydrophobic region show lower R 2 CP values at high dehydration levels. Similar studies in presence of peptides and proteins can give insight into optimized lipid hydration for protein functionality and slow cooperative motions.

NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs

“…It has been reported that this small cationic peptide has antibacterial activity against both Grampositive and Gram-negative bacteria (4,5). The correlation between the structure and the antimicrobial activity of this peptide was previously studied in detail by means of solution and solid-state NMR spectroscopies (6)(7)(8)(9)(10). As part of our efforts to find novel AMPs with better antimicrobial activity than LPcin, we designed 11 LPcin analog peptides and chose three analog peptides that showed the best antibacterial activ-ity, using the agar hole test against five pathogens.…”