Influence of the N-terminus acetylation of Semax, a synthetic analog of ACTH(4-10), on copper(II) and zinc(II) coordination and biological properties

Autor: Antonio Magrì, Irina Naletova, Alessandro Giuffrida, Giovanni Tabbì, Cristina Satriano, Giuseppe Pappalardo, Francesco Attanasio, V. G. Nicoletti

Publikováno v: Journal of inorganic biochemistry 164 (2016): 59–69. doi:10.1016/j.jinorgbio.2016.08.013
info:cnr-pdr/source/autori:Magri, Antonio; Tabbi, Giovanni; Giuffrida, Alessandro; Pappalardo, Giuseppe; Satriano, Cristina; Naletova, Irina; Nicoletti, Vincenzo G.; Attanasio, Francesco/titolo:Influence of the N-terminus acetylation of Semax, a synthetic analog of ACTH(4-10), on copper(II) and zinc(II) coordination and biological properties/doi:10.1016%2Fj.jinorgbio.2016.08.013/rivista:Journal of inorganic biochemistry/anno:2016/pagina_da:59/pagina_a:69/intervallo_pagine:59–69/volume:164

Semax is a heptapeptide (Met-Glu-His-Phe-Pro-Gly-Pro) that encompasses the sequence 4-7 of N-terminal domain of the adrenocorticotropic hormone and a C-terminal Pro-Gly-Pro tripeptide. N-terminal amino group acetylation (Ac-Semax) modulates the chemi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc7688e3674956a8a6eedfc59dfad325
https://pubmed.ncbi.nlm.nih.gov/27586814