New hypothesis on amino acid complementarity and its evaluation on TGF-beta(2)-related peptides

A new hypothesis of amino acid complementarity based on the genetic code pe riodicity is presented and evaluated on the peptide pairs composed of the f ragments of TGF-beta (2) protein (YIGKTPKI and YYIGKTPKIE) and correspondin g complementary peptides [IYPLC(Acm)GLY, IIYTLWGLYL, IIYPLC(Acm)GLYL and II YTLC(Acm)GLYL], The ESI-MS and CD methods were used for monitoring of the c omplexation. It was found that heterodimeric structures are formed between the peptides and complementary peptides, No complexation appears in solutio ns of single components of the systems, nor in solutions containing the mix tures of TGF-beta (2) peptides or complementary peptides, CD measurements s uggest that the conformation of peptides needed for complex formation is of the beta -structure type, The binding forces, which stabilize the complexe s, consist mainly of hydrophobic interactions. Copyright (C) 2000 John Wile y & Sons, Ltd.