Lipid- and sugar-modified endomorphins: novel targets for the treatment of neuropathic pain

Varamini, Pegah and Toth, Istvan (2013) Lipid- and sugar-modified endomorphins: novel targets for the treatment of neuropathic pain. Frontiers in Pharmacology, 4 155: 1-7. doi:10.3389/fphar.2013.00155


Author Varamini, Pegah
Toth, Istvan
Title Lipid- and sugar-modified endomorphins: novel targets for the treatment of neuropathic pain
Journal name Frontiers in Pharmacology   Check publisher's open access policy
ISSN 1663-9812
Publication date 2013-12-13
Sub-type Critical review of research, literature review, critical commentary
DOI 10.3389/fphar.2013.00155
Open Access Status DOI
Volume 4
Issue 155
Start page 1
End page 7
Total pages 7
Editor Susan Hua
Place of publication Lausanne, Switzerland
Publisher Frontiers Research Foundation
Language eng
Formatted abstract
Endomorphins are endogenous opioid peptides that cause potent antinociception in rodent models of acute and neuropathic pain with less undesirable side effects than opioid alkaloids. However, endomorphins are poorly suited to clinical applications because of low membrane permeability and a susceptibility to enzymatic degradation. Glycosylation and lipidation have proven to be two of the most robust approaches for the generation of new therapeutic endomorphin derivatives. Conjugation with lipoamino acids (LAA) confers an amphipathic character to the peptide, which improved interaction between the peptide and the lipid bilayer of the cell membranes, increasing permeability. Glycosylation can also improve peptide stability and blood brain barrier (BBB) transport. It is believed that an endocytotic mechanism (transcytosis) is responsible for the systemic delivery of water-soluble glycopeptides. This review discusses the application of glycosylation and lipidation strategies to improve the drug-like properties of endomorphins. Pharmacologically active endomorphin analogs with less adverse effects are also discussed.
Keyword Endomorphin
Peptide delivery
Neuropathic pain
Lipoamino acid
Glycosylation
Lipopeptide
Glycopeptide
Blood brain barrier
Q-Index Code CX
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Non HERDC
ERA White List Items
School of Chemistry and Molecular Biosciences
School of Pharmacy Publications
 
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Created: Tue, 07 Jan 2014, 21:31:54 EST by Dr Pegah Varamini on behalf of School of Chemistry & Molecular Biosciences