@article {Zhang:2012:0929-8673:1602,
title = "Converting Peptides into Drug Leads by Lipidation",
journal = "Current Medicinal Chemistry",
parent_itemid = "infobike://ben/cmc",
publishercode ="ben",
year = "2012",
volume = "19",
number = "11",
publication date ="2012-04-01T00:00:00",
pages = "1602-1618",
itemtype = "ARTICLE",
issn = "0929-8673",
url = "https://www.ingentaconnect.com/content/ben/cmc/2012/00000019/00000011/art00002",
doi = "doi:10.2174/092986712799945003",
keyword = "peptide selfassembling, ADME, lipidated peptide, lipoamino acids, lipidation, peptide secondary structure, peptide, peptide serum stability, peptide synthesis, peptide SAR",
author = "Zhang, L. and Bulaj, G.",
abstract = "Lipidation is a posttranslational modification of proteins that has also found its use in designing peptide drugs. The presence of a lipid group in peptides modulates their hydrophobicity, secondary structures and self-assembling propensities while retaining their abilities to bind
to target receptors. Lipidation improves peptidesa' metabolic stability, membrane permeability, bioavailability, and changes peptides' pharmacokinetic and pharmacodynamic properties. Herein, we review the applications of various lipidation strategies in peptide drug design, the effects
of the chain length and anchor position of fatty acids in peptide lipidation, the physicochemical and biological properties of selected lipidated peptides and the synthesis strategies for peptide lipidation.",
}