Structural and thermodynamic approach to peptide immunogenicity.

ABSTRACT: In the conventional paradigm of humoral immunity, B cells recognize their cognate antigen target in its native form. However, it is well known that relatively unstable peptides bearing only partial structural resemblance to the native protein can trigger antibodies recognizing higher-order structures found in the native protein. On the basis of sound thermodynamic principles, this work reveals that stability of immunogenic proteinlike motifs is a critical parameter rationalizing the diverse humoral immune responses induced by different linear peptide epitopes. In this paradigm, peptides with a minimal amount of stability (DeltaG(x)<0 kcal/mol) around a proteinlike motif (x) are capable of inducing antibodies with similar affinity for both peptide and native protein, more weakly stable pept

SUBMITTER: Camacho CJ 

PROVIDER: S-EPMC2577884 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature