Conformational dynamics of a short antigenic peptide in its free and antibody bound forms gives insight into the role of β-turns in peptide immunogenicity

What is it about?

Antigen antibody interactions play an important role in the functioning of immune system. In the current context, the antigen is a peptide fragment from influenza hemagglutinin and the antibody is raised against it, which cross reacts with the peptide as part of the protein also as shown in literature. Thus this antipeptide antibody shows cross reactivity with the cognate sequence in parent protein. In this paper, based on computer simulations, we find that the conformation of the peptide recognized by antibody is sampled to a greater extent in hemagglutinin protein at a higher temperature closer to physiological temperature than at room temperature.

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Why is it important?

We think that immunogenicity might be enhanced at a higher temperature, at least in this example, because antibody recognized conformation of the protein is sampled better at this higher temperature.