Abstract
The pressure on researchers to generate publications is increasing and the competition for increasingly scarce resources is bringing this pressure to critical levels. At the same time the web creates new opportunities to communicate, both to other researchers through sharing of things beyond the traditional journal publication, and to the wider community through lower costs of distribution. This is both a benefit, bringing opportunities for new forms of publication and reducing the costs of sharing research outputs like data, software, and research records, and also a burden, as it brings new expectations of the availability of information. The result of these pressures is an explosion of information which challenges our ability to cope. Looking ahead, how can we shape the way that we communicate, and the way that we discover information? What is the optimal design for a system that communicates research effectively and efficiently while allowing researchers to focus on their research?
Highlights
Sortase-Mediated Ligation group, and attachment to the solid support
There remains a significant need for robust and simple methodologies for protein immobilization that can be applied to wide range of proteins and solid supports
Sortases recognise a specific peptide sequence (LPETG for SrtA of S. aureus used in this work) in proteins targeted for covalent attachment to the cell wall peptidoglycan
Summary
Proteins expressed with the C-terminal recognition sequence can be covalently attached to a wide range of constructs with an N-terminal glycine amide motif including peptides [20], PNA [21], full length proteins [22] and small molecule substrates [23]. Another group has independently described an example of Sortase mediated ligation to a beaded solid support [22]. These reactions proceed under aqueous conditions without the addition of any further reagents beyond the protein, ligation substrate, and Sortase. We investigate the ability of S. aureus SrtA to ligate proteins to a range of solid supports
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