In silico analysis of adhesive foot proteins of mussels

Abstract

<span style="font-size:9.0pt;font-family: " times="" new="" roman";mso-fareast-font-family:"times="" roman";mso-bidi-font-family:="" "times="" roman";mso-ansi-language:en-us;mso-fareast-language:en-us;="" mso-bidi-language:ar-sa"="" lang="EN-US">Byssal threads made up of foot proteins help the mussels to colonize new habitats facilitating attachment in aqueous environments. In the current study, we have analyzed mussel adhesive proteins, foot protein 1 (fp1) and foot protein 3 (fp3) in terms of their amino acid composition and dipeptide and tripeptide preferences. Further, analysis of sequence around the post translationally modified fp1 shows a sequential arrangement of decapeptide or octapeptide patterns. The pattern that was derived from four species of <i style="mso-bidi-font-style:normal">Mytilus </i>was "Y-X(5)-Y-X(3)", while the three sequences from <i style="mso-bidi-font-style: normal">Perna virdis</i> show "W-X(2)-W-X(6)" pattern and the four sequences from <i style="mso-bidi-font-style:normal">Perna canaliculus</i> show octapeptide "Y-X(3)-Y-X(3)" pattern repeats. <i style="mso-bidi-font-style: normal">In silico</i> analysis of amino acid composition using PERL program confirms the significant role of amino acid residues. The dipeptide and tripeptide analyses of cement proteins of barnacles and polychaetes were also performed. Dipeptide and tripeptide analysis provided an overview of compositional bias which is prevalent among marine invertebrate adhesive protein complexes. The analyses of three groups of frequent macrofoulers (mussels, barnacles and polychaetes) bring out the importance of individual amino acids and dipeptides and tripeptides in underwater adhesion.</span>