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Synthesis, conformation, and immunoreactivity of new carrier molecules based on repeated tuftsin‐like sequence
Author(s) -
Mezö Gábor,
Kalászi Adrián,
Reményi Judit,
Majer Zsuzsa,
Hilbert Ágnes,
Láng Orsolya,
Köhidai László,
Barna Krisztina,
Gaál Dezsö,
Hudecz Ferenc
Publication year - 2004
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20024
Subject(s) - tuftsin , oligopeptide , pentapeptide repeat , chemistry , tetrapeptide , lysine , chemotaxis , peptide , antibody , residue (chemistry) , sequence (biology) , biochemistry , stereochemistry , microbiology and biotechnology , amino acid , immunology , receptor , biology
Sequential oligopeptides based on a pentapeptide (TKPKG) derived from tuftsin with different lengths were synthesized by stepwise solid phase methodology. These highly soluble oligomers were nontoxic on mouse spleen cells, and other biological data suggested that tuftsin‐like properties were also presented. The (TKPKG) n ( n =2,4,6,8) oligopeptides were not immunogenic; however, they increased sheep red blood cells (SRBC) antigen specific antibody response in mice, demonstrating their immunostimulatory effect. Chemotactic activity was also found on J774 monocyte cells, while MRC5 fibroblasts were chemotactically nonresponders to the tested forms of tuftsin. These oligomers showed unordered and flexible structure by CD measurements, confirmed by computer modeling studies indicating also a fairly good accessibility of the ϵ‐amino group of each lysine residue. Data suggest that these new oligotuftsin derivatives can be considered as promising carriers for synthetic vaccine. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004