Publication: Improving membrane binding as a design strategy for amphipathic peptide hormones: 2-helix variants of PYY3-36
Improving membrane binding as a design strategy for amphipathic peptide hormones: 2-helix variants of PYY3-36
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Pedersen, S. J., Bhatia, V. K., Jurt, S., Paulsson, J. F., Pedersen, M. H., Jorgensen, R., Holst, B., Stamou, D., Vrang, N., Zerbe, O., & Jensen, K. J. (2012). Improving membrane binding as a design strategy for amphipathic peptide hormones: 2-helix variants of PYY3-36. Journal of Peptide Science, 18(9), 579–587. https://doi.org/10.1002/psc.2436
Abstract
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It has been hypothesized that amphipathic peptides might bind to membranes prior to activating their cognate receptors, but this has proven difficult to test. The peptide hormone PYY3-36 is believed to perform its appetite-suppressing actions through binding to hypothalamic Y2 receptors. It has been proposed that PYY3-36 via its amphipathic a-helix binds to the plasma membrane prior to receptor docking. Here, our aim was to study the implication of this hypothesis using new analogs of PYY3-36. We first studied membrane binding of PYY3
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- Bhatia, V K
- Jurt, S
- Paulsson, J F
- Pedersen, M H
- Jorgensen, R
- Holst, B
- Stamou, D
- Vrang, N
- Zerbe, O
- Jensen, K J
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Pedersen, S. J., Bhatia, V. K., Jurt, S., Paulsson, J. F., Pedersen, M. H., Jorgensen, R., Holst, B., Stamou, D., Vrang, N., Zerbe, O., & Jensen, K. J. (2012). Improving membrane binding as a design strategy for amphipathic peptide hormones: 2-helix variants of PYY3-36. Journal of Peptide Science, 18(9), 579–587. https://doi.org/10.1002/psc.2436
