Inner membrane proteins YgdD and SbmA are required for the complete susceptibility of to the proline-rich antimicrobial peptide arasin 1(1-25).

Arasin 1 from the spider crab is a proline-rich antimicrobial peptide (PR-AMP), which kills target bacteria by a non-membranolytic mechanism. By using a fluorescent derivative of the peptide, we showed that arasin 1 rapidly penetrates into cells without membrane damage. To unravel its mode of action, a knockout gene library of was screened and two types of mutants with a less susceptible phenotype to the arasin 1 fragment (1-23) were found.

Structure-activity relationships of the antimicrobial peptide arasin 1 - and mode of action studies of the N-terminal, proline-rich region.

Arasin 1 is a 37 amino acid long proline-rich antimicrobial peptide isolated from the spider crab, Hyas araneus. In this work the active region of arasin 1 was identified through structure-activity studies using different peptide fragments derived from the arasin 1 sequence. The pharmacophore was found to be located in the proline/arginine-rich NH(2) terminus of the peptide and the fragment arasin 1(1-23) was almost equally active to the full length peptide.