Understanding Molecular Complexity in Protein and Peptide-Lipid Systems

Autor: Vian S. Ismail, Hannah M. Britt, John M. Sanderson, Jackie A. Mosely, Aruna S. Prakash
Rok vydání: 2015
Předmět:
Zdroj: Biophysical Journal. 108:552a
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2014.11.3028
Popis: Peptide addition to lipid membranes has been shown in some cases to lead to significant molecular complexity, principally as a consequence of the chemical processes that occur subsequent to the addition (http://dx.doi.org/10.1016/j.jmb.2013.07.013). Foremost amongst these is acyl transfer from lipid constituents of the membrane to acceptor sites on the peptide, generating lipidated peptides and lyso-lipids. As an example, addition of the peptide melittin to a two-component lipid membrane leads to the potential formation of up to 20 different peptide species and 8 different lyso-lipids, many of which have been detected, some in significant quantities. The lipidation by-products, lyso-lipids, may also serve as acyl group donors for further lipidation. This process is not restricted to peptides; some proteins and low molecular weight compounds exhibit the hallmarks of this lipidation activity. In a proof-of-principle study, we have examined the lipidation profiles of candidate proteins and shown that they closely resemble the fatty acyl composition of the membrane in which they are generated, supporting the hypothesis that their lipidation arises from membrane lipid precursors. At the other extreme, low molecular weight compounds have been found to undergo similar lipidation processes. Current work to understand the factors that dictate this reactivity, and the consequences of lipidation, will be discussed.
Databáze: OpenAIRE