Conformation-dependent recognition of HIV gp120 by designed ankyrin repeat proteins provides access to novel HIV entry inhibitors.

@article{Mann2013ConformationdependentRO,
  title={Conformation-dependent recognition of HIV gp120 by designed ankyrin repeat proteins provides access to novel HIV entry inhibitors.},
  author={Axel M. Mann and Nikolas Friedrich and Anders Krarup and Jacqueline Weber and Emanuel Stiegeler and Birgit Dreier and Pavel Pugach and Melissa Robbiani and Tina Riedel and Kerstin Moehle and John Alan Robinson and Peter Rusert and Andreas Pl{\"u}ckthun and Alexandra Trkola},
  journal={Journal of virology},
  year={2013},
  volume={87 10},
  pages={5868-81}
}
Here, we applied the designed ankyrin repeat protein (DARPin) technology to develop novel gp120-directed binding molecules with HIV entry-inhibiting capacity. DARPins are interesting molecules for HIV envelope inhibitor design, as their high-affinity binding differs from that of antibodies. DARPins in general prefer epitopes with a defined folded structure. We probed whether this capacity favors the selection of novel gp120-reactive molecules with specificities in epitope recognition and… CONTINUE READING

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Virology on A ril 27

  • R Pejchal, KJ Doores, +4 authors Mann
  • by U N IV E R S IT A T Z U R IC H
  • 2013
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