Synthesis of Heterobifunctional Protein Fusions Using Copper-Free Click Chemistry and the Aldehyde Tag

Clicking into place: Cu‐free click chemistry is combined with the aldehyde tag protein modification strategy to produce heterobifunctional protein fusions. This method relies on linkers that utilize orthogonal triazole and oxime chemistries (see scheme) to expand on conjugation with the fGly residue...

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Published inAngewandte Chemie (International ed.) Vol. 51; no. 17; pp. 4161 - 4165
Main Authors Hudak, Jason E., Barfield, Robyn M., de Hart, Gregory W., Grob, Patricia, Nogales, Eva, Bertozzi, Carolyn R., Rabuka, David
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 23.04.2012
WILEY‐VCH Verlag
Wiley Subscription Services, Inc
Wiley
EditionInternational ed. in English
Subjects
Aldehydes
Aldehydes - chemistry
Antibodies
BASIC BIOLOGICAL SCIENCES
bioorganic chemistry
Click Chemistry
Communications
Conjugation
Copper - chemistry
Growth Hormone - chemistry
Human
Humans
INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Maltose-Binding Proteins - chemistry
Maltose-Binding Proteins - ultrastructure
Microscopy, Electron, Transmission
Models, Molecular
Molecular Probes - chemical synthesis
Oximes
Protein Structure, Tertiary
Proteins
Residues
Strategy
Triazoles
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Summary:Clicking into place: Cu‐free click chemistry is combined with the aldehyde tag protein modification strategy to produce heterobifunctional protein fusions. This method relies on linkers that utilize orthogonal triazole and oxime chemistries (see scheme) to expand on conjugation with the fGly residue and enables site‐specific protein conjugation to full‐length human antibodies.
Bibliography:NSF
Funded Access
ark:/67375/WNG-SZ0J614B-6
ArticleID:ANIE201108130
We thank Prof. Zev Gartner, Ellen Sletten, Brian Belardi, and Brian Carlson for materials, discussion, and manuscript critique. This work was funded by grants from the NIH to D.R. (1RC1EB010344-01) and C.R.B. (GM59907). J.E.H. was supported by an NSF predoctoral fellowship.
NIH - No. 1RC1EB010344-01; No. GM59907
istex:6676A8CA688D480D102E59C3928FCB3BDF6280B4
We thank Prof. Zev Gartner, Ellen Sletten, Brian Belardi, and Brian Carlson for materials, discussion, and manuscript critique. This work was funded by grants from the NIH to D.R. (1RC1EB010344‐01) and C.R.B. (GM59907). J.E.H. was supported by an NSF predoctoral fellowship.
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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USDOE Office of Science (SC)
National Science Foundation (NSF)
AC02-05CH11231
National Institutes of Health (NIH)
Supporting information for this article is available on the WWW under http://dx.doi.org/10.1002/anie.201108130.
We thank Prof. Zev Gartner, Ellen Sletten, Brian Belardi, and Brian Carlson for materials, discussion, and manuscript critique. This work was funded by grants from the NIH to D.R., (1RC1EB010344-01) and C.R.B. (GM59907). J.E.H. was supported by an NSF predoctoral fellowship.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201108130