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Development of a Multifunctional Benzophenone Linker for Peptide Stapling and Photoaffinity Labelling.

Wu Y, Olsen LB, Lau YH, Jensen CH, Rossmann M, Baker YR, Sore HF, Collins S, Spring DR - Chembiochem (2016)

Bottom Line: We present the design and synthesis of a novel multifunctional benzophenone linker that serves as both a photo-crosslinking motif and a peptide stapling reagent.Using double-click stapling, we attached the benzophenone to the peptide via the staple linker, rather than by modifying the peptide sequence with a photo-crosslinking amino acid.When applied to a p53-derived peptide, the resulting photoreactive stapled peptide was able to preferentially crosslink with MDM2 in the presence of competing protein.

View Article: PubMed Central - PubMed

Affiliation: University Chemical Laboratory, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.

No MeSH data available.


Photoaffinity labelling of MDM2 in the presence of BSA. MDM2 is preferentially labelled by peptide A1; control peptide B1 does not label MDM2. BSA was at 170 μm (+) or 240 μm (++).
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cbic201500648-fig-0002: Photoaffinity labelling of MDM2 in the presence of BSA. MDM2 is preferentially labelled by peptide A1; control peptide B1 does not label MDM2. BSA was at 170 μm (+) or 240 μm (++).

Mentions: In order to determine if the observed crosslinking was specific for MDM2, A1 was incubated with mixtures of MDM2 and bovine serum albumin (BSA). Clear bands reflected preferential labelling of MDM2 by A1 (not B1), and the addition of BSA did not significantly impact the ability of A1 to crosslink to MDM2 (Figure 2).


Development of a Multifunctional Benzophenone Linker for Peptide Stapling and Photoaffinity Labelling.

Wu Y, Olsen LB, Lau YH, Jensen CH, Rossmann M, Baker YR, Sore HF, Collins S, Spring DR - Chembiochem (2016)

Photoaffinity labelling of MDM2 in the presence of BSA. MDM2 is preferentially labelled by peptide A1; control peptide B1 does not label MDM2. BSA was at 170 μm (+) or 240 μm (++).
© Copyright Policy - creativeCommonsBy
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC4862033&req=5

cbic201500648-fig-0002: Photoaffinity labelling of MDM2 in the presence of BSA. MDM2 is preferentially labelled by peptide A1; control peptide B1 does not label MDM2. BSA was at 170 μm (+) or 240 μm (++).
Mentions: In order to determine if the observed crosslinking was specific for MDM2, A1 was incubated with mixtures of MDM2 and bovine serum albumin (BSA). Clear bands reflected preferential labelling of MDM2 by A1 (not B1), and the addition of BSA did not significantly impact the ability of A1 to crosslink to MDM2 (Figure 2).

Bottom Line: We present the design and synthesis of a novel multifunctional benzophenone linker that serves as both a photo-crosslinking motif and a peptide stapling reagent.Using double-click stapling, we attached the benzophenone to the peptide via the staple linker, rather than by modifying the peptide sequence with a photo-crosslinking amino acid.When applied to a p53-derived peptide, the resulting photoreactive stapled peptide was able to preferentially crosslink with MDM2 in the presence of competing protein.

View Article: PubMed Central - PubMed

Affiliation: University Chemical Laboratory, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.

No MeSH data available.