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ID 20570
file
creator
Nokihara, Kiyoshi
Yasuhara, Tadashi
Lerner, Ethan A.
Wray, Victor
subject
vasodilator
maxadilan
PAC1 receptor
disulfide isomer
highly efficient solid-phase synthesis
difficult sequence
melanophore assay
NDC
Medical sciences
abstract
A potent and persistent non-mammalian derived vasodilator, maxadilan (Maxa) consists of 61 amino acids with two disulfide linkages and acts as an agonist of the type I receptor of pituitary adenylate cyclase activating polypeptide (PACAP), although there is very little sequence similarity. The total chemical syntheses of Maxa, its disulfide isomers and various fragments have been performed successfully by highly efficient solid-phase peptide synthesis (SPPS). A "difficult sequence", envisaged in the middle region of Maxa, could be overcome by improved synthesis protocols. After assembly peptides were liberated from the resin by cleavage. Peptides having disulfide(s) were purified by two steps of preparative HPLC using cation exchange followed by reverse phase columns. Purified peptides were characterized by HPLC, Edman-sequencing, amino acid analysis and mass spectrometry in addition to disulfide form determination. The peptides obtained were used for recognition studies by the melanophore assay to confirm the native disulfide form. Peptide libraries related to Maxa, produced in the present study, will be useful for the elucidation of the structural requirements of Maxa for interaction with the PACAP type 1 receptor (PAC1).
journal title
International Journal of Peptide Research and Therapeutics
volume
Volume 13
issue
Issue 1-2
start page
377
end page
386
date of issued
2007-06
publisher
Springer
issn
1573-3149
ncid
publisher doi
language
eng
nii type
Journal Article
HU type
Journal Articles
DCMI type
text
format
application/pdf
text version
author
rights
Copyright (c) 2007 Springer "The original publication is available at www.springerlin.com"
relation url
department
Graduate School of Biomedical Science