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Synthesis and biological activities of new analogues of thymopoietin II (32–36)
Author(s) -
NawrockaBolewska Eleonora,
Siemion Ignacy Z.,
Mihelić Mirna,
Voelter Wolfgang
Publication year - 1990
Publication title -
liebigs annalen der chemie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 0170-2041
DOI - 10.1002/jlac.199019900144
Subject(s) - pentapeptide repeat , chemistry , biological activity , proline , residue (chemistry) , stereochemistry , phagocytosis , amino acid , biochemistry , in vitro , microbiology and biotechnology , peptide , biology
The pentapeptide fragment of thymopoietin II (32–36) (TP5) shows similar biological activities as the parent molecule, also induces E‐rosette formation, and enhances phagocytosis. In order to elucidate further structural and functional requirements for its activity we decided to replace each amino acid residue of the pentapeptide by proline moieties.