The synthesis and structure of an n-terminal dodecanoic acid conjugate of a-conotoxin MII


Autoria(s): Blanchfield, Joanne T.; Dutton, Julie T.; Hogg, R. C.; Craik, D. J.; Adams, D. J.; Lewis, R. J.; Alewood, P.; Toth, I.
Contribuinte(s)

Albericio, Fernando

Fields, Gregg B.

Wade, John D.

Data(s)

01/05/2001

Resumo

The alpha-conotoxin MII is a 16 amino acid long peptide toxin isolated from the marine snail, Conus magus. This toxin has been found to be a highly selective and potent inhibitor of neuronal nicotinic acetylcholine receptors of the subtype alpha3beta2. To improve the bioavailability of this peptide, we have coupled to the N-terminus of conotoxin MII, 2-amino-D,L-dodecanoic acid (Laa) creating a lipidic linear peptide which was then successfully oxidised to produce the correctly folded conotoxin MII construct.

Identificador

http://espace.library.uq.edu.au/view/UQ:64058/UQ_AV_64058.pdf

http://espace.library.uq.edu.au/view/UQ:64058

Idioma(s)

eng

Publicador

Springer-Verlag

Palavras-Chave #Biochemistry & Molecular Biology #Alpha-aminododecanoic #Drug Delivery #Alpha-conotoxin Mii #Lipoamino Acid #Peptide Synthesis #3-dimensional Solution Structure #Phase Peptide-synthesis #Conus Peptides #Receptors #C1 #270104 Membrane Biology #780105 Biological sciences
Tipo

Journal Article