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Synthetic Peptides for the Immunodiagnosis of Human Diseases

“…Lipophilic derivatization [23,30] Covalent attachment of synthetic peptides to immunoassays Covalent immobilization via the peptide amino groups [30,31,36] Covalent immobilization via the peptide carboxy groups [37] Approaches for increasing the antigenicity of peptide sequences…”

“…Usually peptides do not have the same conformation free in solution as when adsorbed or covalently coupled to microtiter plates, the orientation of an immobilized antigen being important for recognition by an antibody. A strategy to overcome the low coating efficiency of highly hydrophilic peptides to microtiter plates and to avoid unpredictable orientation of the peptides on the surface is based on the covalent attachment of the synthetic peptides to the immunoassay surfaces [30][31][32][33][34][35][36]. Covalent binding, unlike simple physical binding, may orientate the immobilized peptides in a defined way on the solid phase.…”

Filaggrin Peptides with β‐Hairpin Structure Bind Rheumatoid Arthritis Antibodies

“…[7][8][9] It is evident that the essential hapten for the binding of the antibody is the urea group present in citrulline, because mutants with the isosteric amino acid arginine are not detected. [1,2,10] Since cfc1-cyc 1 does not have a preferred conformation, the geometry of the binding epitope is still speculative (vide infra). If the disulfide macrocyclization already leads to an improved binding of the antibody, additional structural restriction of the epitope and the impact on selectivity and affinity has to be investigated.…”

“…In conclusion, the peptide conformation is based mainly on the disulfide bridge and hydrophobic interaction between Trp 6 and Leu 15 . The bI'/bII'-flip of the b-turn in the rigid hairpin of 4 leads to exchange broadening of the amide protons of Gly 11 and Cit 10 . With either the amino acids Ala (peptide 9) or d-Ala (peptide 10) at the position of Gly 11 , one b-turn structure is energetically favored, wherein d-Ala forms a bII'-turn.…”

Filaggrin‐Peptide mit β‐Haarnadel‐Struktur binden Rheuma‐Antikörper

“…[7][8][9] Es gilt als gesichert, dass Citrullin durch die Harnstofffunktion das für die Antikçrperbindung essenzielle Hapten trägt, weil Mutanten mit der isosteren Aminosäure Arginin nicht erkannt werden. [1,2,10] Über die Geometrie der Bindung konnte bisher nur spekuliert werden, da das Cyclopeptid 1 keine erkennbare Vorzugskonformation aufweist. Wenn bereits die Makrocyclisierung durch ein Disulfid zur Erhçhung der Antikçrperbindung führt, dann gilt es zu untersuchen, ob die weitere strukturelle Restriktion des Epitops zu einem weiteren Gewinn an Selektivität und Affinität führt.…”