Synthesis, Purification and Surface Activities of the Human Pulmonary Surfactant Protein-C(SP-C)Analogue, SP-CL16(6-28)

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We previously reported that a human analogue of pulmonary surfactant protein-C(SP-C), SP-CL16(6-28), with 23 residues(Fig.1)was the most active analogue in a reconstituted lipid mixture and had the shortest chain among the poly-leucine-analogues examined. In the present study, we examined a new method of preparing this analogue, that is, stepwise solid-phase synthesis employing the Fmoc method followed by centrifugal partition chromatography(CPC)using an n-hexane/CH_3 OH/H_2O/trifluoroacetic acid(TFA)(1000:1000:1:2, v/v)solvent system according to the descending method. The synthetic peptides were identified by matrix-assisted laser desorption ionization time-of-flight(MALDI-TOF)mass spectrometry in search of activity to improve the in vitro surface activity of a ternary lipid mixture composed of dipalmitoylphosphatidylcholine, egg-phosphatidylglycerol and palmitic acid(75:25:10, w/w)in a Langmuir-Wilhelmy surface balance. SP-CL16(6-28)seemed comparable in surface activity with Surfacten^<[○!R]>(Surfactant-TA), a modified surfactant preparation which has been used for the treatment of respiratory distress syndrome.
公益社団法人日本薬学会の論文
2001-12-01