Antibody-unfolding and metastable-state binding in force spectroscopy and recognition imaging.

ABSTRACT: Force spectroscopy and recognition imaging are important techniques for characterizing and mapping molecular interactions. In both cases, an antibody is pulled away from its target in times that are much less than the normal residence time of the antibody on its target. The distribution of pulling lengths in force spectroscopy shows the development of additional peaks at high loading rates, indicating that part of the antibody frequently unfolds. This propensity to unfold is reversible, indicating that exposure to high loading rates induces a structural transition to a metastable state. Weakened interactions of the antibody in this metastable state could account for reduced specificity in recognition imaging where the loading rates are always high. The much weaker interaction between the p

SUBMITTER: Kaur P 

PROVIDER: S-EPMC3010837 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature