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Sequencing and synthesis of pardaxin, a polypeptide from the Red Sea Moses sole with ionophore activity
Author(s) -
Shai Yechiel,
Fox Jay,
Caratsch Carlo,
Shih Yu-Liang,
Edwards Charles,
Lazarovici Philip
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81007-x
Subject(s) - chemistry , stereochemistry , ionophore , biochemistry , membrane
Pardaxin, an amphipathic polypeptide secreted by the Red Sea flatfish Pardachirus marmoratus whose sequence is NH 2 ‐G‐F‐F‐A‐L‐I‐P‐K‐I‐I‐S‐S‐P‐L‐F‐K‐T‐L‐L‐S‐A‐V‐G‐S‐A‐L‐S‐S‐S‐G‐G‐Q‐E, was synthesized by the solid‐phase method. The structure was verified by sequencing. The synthetic polypeptide changed the resistance of lipid bilayers by forming pores. At 10 −7 −10 −8 M, the synthetic pardaxin increased the frequency of the spontaneous release of quanta of acetylcholine at the neuromuscular junction by up to 100‐fold, resembling the native product. Synthetic pardaxin seems to be a suitable tool for investigating the molecular structures underlying channel selectivity.