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Amphiphilic cationic peptides mediate cell adhesion to plastic surfaces
Author(s) -
Rideout Darryl C.,
Lambert Michael,
Kendall Debra A.,
Moe Gregory R.,
Osterman David G.,
Tao H. P.,
Weinstein I. Bernard,
Kaiser E. T.
Publication year - 1985
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041240302
Subject(s) - cationic polymerization , amphiphile , adhesion , cell adhesion , chemistry , cell , microbiology and biotechnology , peptide , biophysics , biochemistry , polymer chemistry , biology , polymer , organic chemistry , copolymer
Four amphiphilic peptides, each with net charges of +2 or more at neutrality and molecular weights under 4 kilodaltons, were found to mediate the adhesion of normal rat kidney fibroblasts to polystyrene surfaces. Two of these peptides, a model for calcitonin (peptide 1, MCT) and melittin (peptide 2, MEL), form amphiphilic α‐helical structures at aqueous/nonpolar interfaces. The other two, a luteinizing hormone‐releasing hormone model (peptide 3, LHM) and a platelet factor model (peptide 4, MPF) form β‐strand structures in amphiphilic environments. Although it contains only 10 residues, LHM mediated adhesion to surfaces coated with solutions containing as little as 10 pmoles/ml of peptide. All four of these peptides were capable of forming monolayers at air‐buffer interfaces with collapse pressures greater than 20 dynes/cm. None of these four peptides contains the tetrapeptide sequence Arg‐Gly‐Asp‐Ser, which has been associated with fibronectin‐mediated cell adhesion. Ten polypeptides that also lacked the sequence Arg‐Gly‐Asp‐Ser but were nonamphiphilic and/or had net charges less than +2 at neutrality were all incapable of mediating cell adhesion (Pierschbacher and Ruoslahti, 1984). The morphologies of NRK cells spread on polystyrene coated with peptide LHM resemble the morphologies on fibronectin‐coated surfaces, whereas cells spread on surfaces coated with MCT or MEL exhibit strikingly different morphologies. The adhesiveness of MCT, MEL, LHM, and MPF implies that many amphiphilic cationic peptides could prove useful as well defined adhesive substrata for cell culture and for studies of the mechanism of cell adhesion.