Pierschbacher M, Hayman E G, Ruoslahti E
Proc Natl Acad Sci U S A. 1983 Mar;80(5):1224-7. doi: 10.1073/pnas.80.5.1224.
Four synthetic peptides that together constitute the cell attachment domain of fibronectin [Pierschbacher, M.D., Ruoslahti, E., Sundelin, J., Lind, P. & Peterson, P. (1982) J. Biol. Chem. 257, 9593-9597] were constructed and tested for their ability to induce cell attachment and spreading. One of these peptides, consisting of the 30 amino acid residues nearest the COOH terminus of the domain, contained all of the cell attachment activity of the whole domain. Under suitable conditions the peptide was approximately as active as intact fibronectin on a molar basis. The activity could be demonstrated by binding the peptide to polystyrene directly, or via albumin, or by coupling it to agarose beads. This synthetic peptide will be useful in the elucidation of the molecular details of the attachment of cells to fibronectin and could allow manipulation of the adhesive properties of cell culture surfaces and prosthetic materials.
构建了四条共同构成纤连蛋白细胞黏附结构域的合成肽段[皮尔斯巴赫，医学博士，罗斯拉蒂，E.，松德林，J.，林德，P. & 彼得森，P.（1982年）《生物化学杂志》257卷，9593 - 9597页]，并测试了它们诱导细胞黏附和铺展的能力。其中一条肽段由该结构域最靠近COOH末端的30个氨基酸残基组成，具备整个结构域的所有细胞黏附活性。在合适条件下，该肽段在摩尔基础上的活性与完整的纤连蛋白大致相当。通过将肽段直接结合到聚苯乙烯上、或通过白蛋白结合、或与琼脂糖珠偶联，均可证明其活性。这种合成肽将有助于阐明细胞与纤连蛋白黏附的分子细节，并可用于操控细胞培养表面和假体材料的黏附特性。
