Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments

Interaction of epitope-related and -unre

Interaction of epitope-related and -unrelated peptides with anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab fragment

✍ Karin Welfle; Rolf Misselwitz; Wolfgang Höhne; Heinz Welfle 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 147 KB

## Abstract The binding of four epitope‐related peptides and three library‐derived, epitope‐unrelated peptides of different lengths (10–14 amino acids) and sequence by anti‐p24 (HIV‐1) monoclonal antibody CB4‐1 and its Fab fragment was studied by isothermal titration calorimetry. The binding consta