Fully synthetic immunogens. Part II. Studies on parallel dimerization of the human IgG1 hinge-fragment 225-232 with N- or C-terminal gastrin related extensions.
The bis-cysteinyl hinge-fragment 225-232 of human IgG1 has been extended at the N- or C-terminus with Nle15-desamido-human-little-gastrin-[5-17] and Nle15-human-little-gastrin-[5-17]-NH2, respectively. Thermodynamically controlled air oxidation of the resulting bis-cysteinyl-peptides led to the predominant formation of the corresponding dimers in parallel alignment despite the incorporation of the immunoglobulin-unrelated gastrin-sequences. These surprising results confirm the high degree of structural information inherent in the hinge-sequence and its intrinsic tendency to fold into the correct structure in terms of cysteine pairings. This protein subdomain-the hinge-peptide-is therefore well suited as core molecule for the design of fully synthetic immunogens with multiple attachment of antigenic determinants.
Wünsch
E
E
Max Planck Institute of Biochemistry, Department of Peptide Chemistry, Martinsried, FRG.
Moroder
L
L
Göhring-Romani
S
S
Musiol
H J
HJ
Göhring
W
W
Scharf
R
R
D000595:Amino Acid Sequence; D000941:Antigens / Q000138:chemical synthesis* / Q000737:chemistry; D005755:Gastrins / Q000138:chemical synthesis / Q000737:chemistry / Q000276:immunology; D006801:Humans; D007074:Immunoglobulin G / Q000138:chemical synthesis / Q000737:chemistry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry / Q000276:immunology; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000276:immunology; D011487:Protein Conformation
D000941:Antigens; D005755:Gastrins; D007074:Immunoglobulin G; D010446:Peptide Fragments; D010455:Peptides