Synthesis and studies on the biophysical activity of human lung surfactant peptide SP-C and its N-terminal fragments.
Human lung surfactant peptide SP-C and two of its N-terminal fragments were prepared by SPPS and their biophysical activities investigated in vitro using a pulsating bubble surfactometer. These studies demonstrated that even low doses of the synthetic peptides with the natural human sequence of SP-C in combination with reconstituted lipid mixtures causes a drastic decrease of surface tension.
Schröder
C
C
Abteilung für Physikalische Biochemie des Physiologisch-chemischen Institut, Universität Tübingen, Germany.
Günther
A
A
Seeger
W
W
Voelter
W
W
D000595:Amino Acid Sequence; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D011510:Proteolipids / Q000138:chemical synthesis* / Q000737:chemistry*; D011663:Pulmonary Surfactants / Q000138:chemical synthesis* / Q000737:chemistry*; D016415:Sequence Alignment
D010446:Peptide Fragments; D011510:Proteolipids; D011663:Pulmonary Surfactants