Structure–antiviral activity relationships of cecropin A‐magainin 2 hybrid peptide and its analogues

Abstract

In order to elucidate the structure-antiviral activity relationship of cecropin A (1-8)-magainin 2 (1-12) (termed CA-MA) hybrid peptide, several analogues with amino acid substitutions were synthesized. In a previous study, it was shown that serine at position 16 in CA-MA hybrid peptide was very important for antimicrobial activity. Analogues were designed to increase the hydrophobic property by substituting a hydrophobic amino acid residue (S --> A, V, F or W, position 16) in the CA-MA hybrid peptide. In this study, the structure-antiviral activity relationships of CA-MA and its analogues were investigated. In particular, substitution of Ser with a hydrophobic amino acid, Val, Phe or Trp at position 16 caused a dramatic increase in the virus-cell fusion inhibitory activity. These results suggested that the hydrophobicity at position 16 in the hydrophobic region of CA-MA is important for potent antiviral activity.

Antimicrobial peptides as new recognition molecules for screening challenging species

“…Although assays were less sensitive for VEE, detection limits for VEE in the AMP-based assays were similar to or better than those of competing cell-or antibodybased technologies [21,22,24,25]. Several groups have previously described the antiviral effects of various AMPs and their derivatives on vaccinia virus [26][27][28]. Most relevant to the present study is a cecropin Amagainin-2 hybrid peptide (CA (1-8)-MA(1-12)) which was shown to exhibit antiviral effects in other studies [26].…”

“…Several groups have previously described the antiviral effects of various AMPs and their derivatives on vaccinia virus [26][27][28]. Most relevant to the present study is a cecropin Amagainin-2 hybrid peptide (CA (1-8)-MA(1-12)) which was shown to exhibit antiviral effects in other studies [26]. The three cecropins (with identical sequences in the first 8 amino acids) exhibited varying affinities for vaccinia virus in the present study, thereby implicating the positions of charged residues and lengths of hydrophobic segments within the C-terminal sequences for these differences.…”

Structural and Functional Characterization of a Multifunctional Alanine-Rich Peptide Analogue from Pleuronectes americanus

“…This is possibly due to the presence of hydrophobic amino acid residues, which might interact with the viral envelope and also with phospholipids encountered on the viral surface [65], [66]. Previous descriptions showed various antiviral peptides that presented directly proportional activity in relation to the hydrophobic ratio, suggesting that hydrophobic and aromatic residues are also important for antiviral activity.…”

Inhibition of Plant-Pathogenic Bacteria by Short Synthetic Cecropin A-Melittin Hybrid Peptides

“…However, major concerns about the use of cecropin A as a pesticide in plant protection are the high production cost of such a long peptide and its sensitivity to protease degradation. Searches for shorter, more potent, nontoxic, and more stable peptides have led to the identification of synthetic peptides with broader and higher activity than their natural counterparts (3,5,6,8,16,17,19,23,33,41,50). In particular, the 11-residue sequence WKLFKKI LKVL-NH 2 (Pep3), derived from the well-known cecropin A(1-7)-melittin(2-9) hybrid peptide (8,17,23), is sufficient for antifungal and antibacterial activities (4,16).…”