| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2006299 | Peptides | 2013 | 5 Pages |
Abstract
⺠PP, PYY and NPY can adopt a highly organized tertiary structure, the PP-fold. ⺠PP-fold structure has long been assumed to be the active conformation of this family of peptides. ⺠Cyclic analogs of PP and PYY, locked in the PP-fold were produced. ⺠Analogs had similar receptor affinity and biological activity to native peptides. ⺠Results suggest the PP-fold may well constitute the active form of the peptides.
Keywords
NPYNeuropeptide Y2 receptorpIC50PYYPMSFHEKHEPESPEInuclear magnetic resonance4-(2-hydroxyethyl)-1-piperazineethanesulfonic acidBSAcDNAphenylmethanesulfonylfluoridew/vbovine serum albumincomplementary deoxyribonucleic acidanalysis of varianceANOVATertiaryNMRsubcutaneousProtein structuresulfhydrylMALDI MSFood intake regulationPancreatic polypeptidepolyethyleneiminepeptide YYpeptide tyrosine tyrosinehigh-performance liquid chromatographyHPLChuman embryonic kidneyNeuropeptide Y
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Authors
Natacha Germain, James S. Minnion, Tricia Tan, Joyceline Shillito, Clare Gibbard, Mohammad Ghatei, Stephen Bloom,