Abstract:
:Magainins are a family of antimicrobial peptides present in the skin extracts of Xenopus laevis. Both magainin-1 and -2 do not have any significant effect on the activity of protein kinase C (PKC). Magainin-2 was found to be readily phosphorylated by PKC to 0.5 mol 32P/mol of peptide. Neither magainin-1, which has a sequence of S8AGK and not S8AKK as in the case of magainin-2, nor the magainin-2 analogue with substitution of Ala for Ser8 was phosphorylated by the kinase, suggesting that Ser8 is the phosphorylation site of magainin-2. One synthetic analogue of magainin, designated magainin B, which has a greater tendency for alpha-helix formation in non-aqueous environment than the parent peptide resulting from substitution of Ser8, Gly13, and Gly18 with Ala in magainin-2-amide, is a potent inhibitor of PKC. This peptide inhibits all three PKC isozymes with IC50 less than 20 microM. Magainin B also inhibits the binding of [3H]phorbol 12,13-dibutyrate to the kinase. These results suggest that magainin-2 may be modified by PKC through phosphorylation and that certain synthetic analogues of magainins may be used as inhibitors of PKC.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Nakabayashi H,Brown JH,Morell JL,Chen HC,Huang KPdoi
10.1016/0014-5793(90)80307-5subject
Has Abstractpub_date
1990-07-02 00:00:00pages
135-8issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(90)80307-5journal_volume
267pub_type
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