✦ LIBER ✦

Abstracts of Poster Section A

Publisher: Wiley (John Wiley & Sons)
Year: 2005
Tongue: English
Weight: 580 KB
Volume: 80
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.20323

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✦ Synopsis

Proteomics relies on 2D, comparative, electrophoresis of labelled proteomes allowing protein profiles to be determined in response to cellular stimulation. A key requirement is to efficiently label the cell proteome population with specific fluorophores in such a way that their mobilities and properties are not altered. The objective of this work was to develop a method to control site specific labelling of proteins and peptides that would enhance current techniques in this field (e.g. 2D difference gel electrophoresis). The project was based on carboxy terminal sequencing, which provides an elegant method of converting a C-terminal amino acid into a good leaving group and thus a handle for attaching a fluorophore. Thiohydantoins were displaced with amines, hydrazines, hydrazides and thiols. This also gave access to a new route to synthesise peptide thioesters and thus native chemical ligation.

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