Crumpled structure of the custom hydrophobic lytic peptide cecropin B3.
The solution structure of a custom lytic peptide, cecropin B3 (CB3), having two identical hydrophobic segments on both the N- and C-termini, was investigated by two-dimensional NMR spectroscopy. The need to determine the structure of this peptide is rooted in its specific ability to lyse lipid layers that have a high content of anionic lipid. The lytic activities of CB3 on cell membranes including cancer cells and bacteria is found to be less than cecropin B1. The results show that CB3 has four discrete segments forming alpha helical structures. The crumpled structure of CB3 provides evidence for the lysis of the lipid layer being via a pathway that differs from pore formation. The results in this study provide strong clues towards a rational design for a potent antimicrobial and antitumor peptide.
Srisailam
S
S
Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan.
Kumar
T K
TK
Arunkumar
A I
AI
Leung
K W
KW
Yu
C
C
Chen
H M
HM
D016475:3T3 Cells; D000595:Amino Acid Sequence; D000818:Animals; D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry; D002942:Circular Dichroism; D004305:Dose-Response Relationship, Drug; D018922:HL-60 Cells; D006801:Humans; D020128:Inhibitory Concentration 50; D019476:Insect Proteins / Q000737:chemistry*; D019169:Jurkat Cells; D020014:K562 Cells; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D008823:Micelles; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010452:Peptide Biosynthesis; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
D000894:Anti-Inflammatory Agents, Non-Steroidal; D023181:Antimicrobial Cationic Peptides; D019476:Insect Proteins; D008823:Micelles; D010455:Peptides; C115151:cecropin B3 protein, insect; C401925:cecropin C