Reversal of linking a sugar on the cysteine thiol of a protein through dibromomaleimideEnglish chemist has found a 'hook' that allows some simple new molecules to be attached to proteins and then transferred, at present this is something that is difficult to accept.
This system, based on a well-established interaction of the amino acid cysteine with maleimides, as well as providing an extra point of attachment so that the two molecules can be buttoned on a single protein that will be released again.
Attachment of compounds in several proteins, termed biokonjugasi, has several important applications, such as allowing multiple proteins to be attached so that their condition will be included in a cell. Amino acid cysteine has an attractive chemicals in the paste to bridge several molecules such as maleimide imide is not saturated. Conversely, other compounds can be attached to the maleimide. However, this attachment can not be changed and in most situations it is highly desirable to move the biokonjugant - as examples of instantaneous release that achieve certain goals in his cell.
Have now a team at University College London, led by Stephen Caddick and James Baker have shown that the modified maleimides can be tied in reverse on some proteins and also provide an extra fastener attached to the next molecule.
'We have made something very simple and very closely linked to maleimide except those containing halogens,' Caddick said. Maleimides contains a five-member ring, which becomes tersaturisasi when molecules interact with cysteine, making this reaction is effectively irreversible. Bromomaleimides, however, hold a double bond in the ring when they're paired with cysteine. This allows for reduced and released from the protein.
Maleimide which was replaced with a single bromine produces a single molecule with two attachment points - one for protein and one for the molecules to be attached. When the two bromines incorporated into the maleimide, and dibromomaleimide, an extra point of attachment included. 'So you can put molecules on protein cysteine residues and then have the capacity for two further molecules to be attached - such as fluorescent dye and peptides, "says Baker.
A key aspect of this system is bromomaleimide can be released under conditions found in sitoplasm in the cell. 'It can provide a way to bring the prodrug into a cell, "says Caddick,' which requires the release of a compound for the drug to be enabled. '
Steve Archibald, namely biokonjugasi researchers at the University of Hull in England, says this approach is an 'elegant and flexible - in fact that this type of procedure that can be found widespread use in the modification of proteins. This is a superior quality of science. '
This system, based on a well-established interaction of the amino acid cysteine with maleimides, as well as providing an extra point of attachment so that the two molecules can be buttoned on a single protein that will be released again.
Attachment of compounds in several proteins, termed biokonjugasi, has several important applications, such as allowing multiple proteins to be attached so that their condition will be included in a cell. Amino acid cysteine has an attractive chemicals in the paste to bridge several molecules such as maleimide imide is not saturated. Conversely, other compounds can be attached to the maleimide. However, this attachment can not be changed and in most situations it is highly desirable to move the biokonjugant - as examples of instantaneous release that achieve certain goals in his cell.
Have now a team at University College London, led by Stephen Caddick and James Baker have shown that the modified maleimides can be tied in reverse on some proteins and also provide an extra fastener attached to the next molecule.
'We have made something very simple and very closely linked to maleimide except those containing halogens,' Caddick said. Maleimides contains a five-member ring, which becomes tersaturisasi when molecules interact with cysteine, making this reaction is effectively irreversible. Bromomaleimides, however, hold a double bond in the ring when they're paired with cysteine. This allows for reduced and released from the protein.
Maleimide which was replaced with a single bromine produces a single molecule with two attachment points - one for protein and one for the molecules to be attached. When the two bromines incorporated into the maleimide, and dibromomaleimide, an extra point of attachment included. 'So you can put molecules on protein cysteine residues and then have the capacity for two further molecules to be attached - such as fluorescent dye and peptides, "says Baker.
A key aspect of this system is bromomaleimide can be released under conditions found in sitoplasm in the cell. 'It can provide a way to bring the prodrug into a cell, "says Caddick,' which requires the release of a compound for the drug to be enabled. '
Steve Archibald, namely biokonjugasi researchers at the University of Hull in England, says this approach is an 'elegant and flexible - in fact that this type of procedure that can be found widespread use in the modification of proteins. This is a superior quality of science. '
Simon Hadlington
Reference
F E B Smith et al, J. Am. Chem. Soc., 2010, DOI: 10.1021/ja908610s
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