Appelt Christian, Wessolowski Axel, Dathe Margitta, Schmieder Peter
Leibnizinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Str. 10, D-13125 Berlin, Germany.
J Pept Sci. 2008 Apr;14(4):524-7. doi: 10.1002/psc.924.
New antimicrobial compounds are of major importance because of the growing problem of bacterial resistance. In this context, antimicrobial peptides have received a lot of attention. Their mechanism of action, however, is often obscure. Here, the structures of two cyclic, antimicrobial peptides from the family of arginine- and tryptophan-rich peptides determined in a membrane-mimicking environment are described. The sequence of the peptides has been obtained from a cyclic parent peptide by scrambling the amino acids. While the activity of the peptides is similar to that of the parent peptide, the structures are not. The peptides do, however, all adopt an amphiphilic structure. A comparison between the structures helps to define the requirements for the activity of these peptides.
由于细菌耐药性问题日益严重，新型抗菌化合物具有至关重要的意义。在此背景下，抗菌肽受到了广泛关注。然而，它们的作用机制往往并不明确。本文描述了在模拟膜环境中测定的两种来自富含精氨酸和色氨酸肽家族的环状抗菌肽的结构。这些肽的序列是通过对环状母肽的氨基酸进行重排而获得的。虽然这些肽的活性与母肽相似，但其结构却不同。不过，这些肽均呈现两亲性结构。结构之间的比较有助于确定这些肽活性的必要条件。
