Premium
New hypothesis on amino acid complementarity and its evaluation on TGF‐β 2 ‐related peptides
Author(s) -
Siemion Ignacy Z.,
ZbozieńPacamaj Renata,
Stefanowicz Piotr
Publication year - 2000
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/1099-1352(200101/02)14:1<1::aid-jmr512>3.0.co;2-p
Subject(s) - complementarity (molecular biology) , peptide , amino acid , chemistry , amino acid residue , genetic code , peptide sequence , biochemistry , combinatorial chemistry , biology , gene , genetics
A new hypothesis of amino acid complementarity based on the genetic code periodicity is presented and evaluated on the peptide pairs composed of the fragments of TGF‐β 2 protein (YIGKTPKI and YYIGKTPKIE) and corresponding complementary peptides [IYPLC(Acm)GLY, IIYTLWGLYL, IIYPLC(Acm)GLYL and IIYTLC(Acm)GLYL]. The ESI‐MS and CD methods were used for monitoring of the complexation. It was found that heterodimeric structures are formed between the peptides and complementary peptides. No complexation appears in solutions of single components of the systems, nor in solutions containing the mixtures of TGF‐β 2 peptides or complementary peptides. CD measurements suggest that the conformation of peptides needed for complex formation is of the β‐structure type. The binding forces, which stabilize the complexes, consist mainly of hydrophobic interactions. Copyright © 2000 John Wiley & Sons, Ltd. Abbreviations used: ACTH corticotrophin.