INTERACTION OF THE 47-KDA TALIN FRAGMENT AND THE 32-KDA VINCULIN FRAGMENT WITH ACIDIC PHOSPHOLIPIDS - A COMPUTER-ANALYSIS

In recent in vitro experiments, it has been demonstrated that the 47-k Da fragment of the talin molecule and the 32-kDa fragment of the vincu lin molecule interact with acidic phospholipids. By using a computer a nalysis method, we determined the hydrophobic and amphipathic stretche s of these fragments and, by applying a purpose-written matrix method, we ascertained the molecular amphipathic structure of alpha-helices. Calculations for the 47-kDa mouse talin fragment (residues 1-433; NH2- terminal region) suggest specific interactions of residues 21-39, 287- 342, and 385-406 with acidic phospholipids and a general lipid-binding domain for mouse talin (primary amino acid sequence 385-401) and for Dictyostelium talin (primary amino acid sequence 348-364). Calculation s for the 32-kDa chicken embryo vinculin fragment (residues 858-1066; COOH-terminal region) and from nematode vinculin alignment indicate fo r chicken embryo vinculin residues 935-978 and 1020-1040 interactions with acidic phospholipids. Experimental confirmation has been given fo r vinculin (residues 916-970), and future detailed experimental analys es are now needed to support the remaining computational data.