caa a22 4500 397555989 CHVBK 20180308164802.0 cr unu---uuuuu 161202e199601 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021213 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021213 Acylation of the α Group in Neuropeptide Y(12-36) Increases Binding Affinity for the Y2 Receptor [Elektronische Daten] [Sachiko Murase, Noboru Yumoto, Michael G. Petukhov, Susumu Yoshikawa] Competition assays using three series of analogs of neuropeptide Y (NPY) ([Xaa11]NPY(ll-36), [Xaa12]NPY(12-36), and [Xaa13]NPY(13-36) revealed that the binding affinity for the Y2 receptor was considerably lowered by truncation of residue 11. Upon acetylation or succinylation of the α-amino group, the binding affinity of [Xaa12]NPY(12-36) recovered to a level similar to that of [Xaa11]NPY(ll-36). No significant difference was observed between the increases caused by acetylation and those caused by succinylation, suggesting that the increase in binding affinity cannot be explained by the change in the net charge at the N-terminus as a consequence of the modification. The scattered data points on a plot of the α-helix content vs. IC50 of all these analogs revealed the absence of any apparent relationship, an indication that prior formation of the α-helix is not necessary for binding to the Y2 receptor. It has been widely accepted that fewer than 12 residues from the C-terminus are directly involved in binding of NPY to the Y2 receptor, while the remaining part of NPY only assists in the adoption of a favorable conformation by the C-terminal hexapeptide for recognition by the receptor. However, the present results suggest that the region around residue 12 does not project from the Y2 receptor. © by the Journal of Biochemistry Regular Papers nationallicence acylation nationallicence aαhelix stability nationallicence binding affinity nationallicence neuropeptide Y nationallicence Y2 receptor nationallicence Murase Sachiko Osaka National Research Institute, AIST, 1-8-31 Midorigaoka, Ikeda, Osaka 563 aut Yumoto Noboru Osaka National Research Institute, AIST, 1-8-31 Midorigaoka, Ikeda, Osaka 563 aut Petukhov Michael G. Osaka National Research Institute, AIST, 1-8-31 Midorigaoka, Ikeda, Osaka 563 aut Yoshikawa Susumu Osaka National Research Institute, AIST, 1-8-31 Midorigaoka, Ikeda, Osaka 563 aut The Journal of Biochemistry Oxford University Press 119/1(1996-01), 37-41 0021-924X 119:1<37 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021213 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021213 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Murase Sachiko Osaka National Research Institute, AIST, 1-8-31 Midorigaoka, Ikeda, Osaka 563 aut NATIONALLICENCE 700 1- Yumoto Noboru Osaka National Research Institute, AIST, 1-8-31 Midorigaoka, Ikeda, Osaka 563 aut NATIONALLICENCE 700 1- Petukhov Michael G. Osaka National Research Institute, AIST, 1-8-31 Midorigaoka, Ikeda, Osaka 563 aut NATIONALLICENCE 700 1- Yoshikawa Susumu Osaka National Research Institute, AIST, 1-8-31 Midorigaoka, Ikeda, Osaka 563 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/1(1996-01), 37-41 0021-924X 119:1<37 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford