Lebetin peptides, a new class of potent aggregation inhibitorsLebetin peptides, a new class of potent aggregation inhibitors

Structural highlights

1q01 is a 1 chain structure with sequence from Macrovipera lebetinus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 24 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LEB_MACLB Lebetins inhibit platelet aggregation induced by thrombin, collagen and PAF-acether. Human platelet aggregation induced by thrombin is inhibited by synthetic lebetin-1-alpha, lebetin-1-beta, lebetin-1-gamma, lebetin-2-alpha and lebetin-2-beta with IC(50) values of 140, 32, 5, 2.5 and 2.8 nM, respectively. Lebetins also inhibit fibrinogen-induced aggregation of alpha-chymotrypsin-treated platelets as well as in vivo collagen-induced thrombocytopenia in rats. Lebetins are not toxic upon intravenous injection into mice and rats.[1] [2] [3]

References

  1. Marrakchi N, Mabrouk K, Regaya I, Sarray S, Fathallah M, Rochat H, El Ayeb M. Lebetin peptides: potent platelet aggregation inhibitors. Haemostasis. 2001 May-Dec;31(3-6):207-10. PMID:11910186 doi:http://dx.doi.org/48064
  2. Barbouche R, Marrakchi N, Mansuelle P, Krifi M, Fenouillet E, Rochat H, el Ayeb M. Novel anti-platelet aggregation polypeptides from Vipera lebetina venom: isolation and characterization. FEBS Lett. 1996 Aug 19;392(1):6-10. PMID:8769304
  3. Barbouche R, Marrakchi N, Mabrouk K, Krifi MN, Van Rietschoten J, Fenouillet E, El Ayeb M, Rochat H. Anti-platelet activity of the peptides composing the lebetin 1 family, a new class of inhibitors of platelet aggregation. Toxicon. 1998 Dec;36(12):1939-47. PMID:9839678
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