TY - JOUR
T1 - Sulfated ligands for the copper(I)-catalyzed azide-alkyne cycloaddition
AU - Wang, Wei
AU - Hong, Senglian
AU - Tran, Andrew
AU - Jiang, Hao
AU - Triano, Rebecca
AU - Liu, Yi
AU - Chen, Xing
AU - Wu, Peng
PY - 2011/10/4
Y1 - 2011/10/4
N2 - The copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC), the prototypical reaction of click chemistry, is accelerated by tris(triazolylmethyl)amine-based ligands. Herein, we compare two new ligands in this family-3-[4-({bis[(1-tert-butyl-1H-1,2,3-triazol-4-yl)methyl]amino}methyl)- 1H-1,2,3-triazol-1-yl]propanol (BTTP) and the corresponding sulfated ligand 3-[4-({bis[(1-tert-butyl-1H-1,2,3-triazol-4-yl)methyl]amino}methyl)-1H-1,2, 3-triazol-1-yl]propyl hydrogen sulfate (BTTPS)-for three bioconjugation applications: 1)labeling of alkyne-tagged glycoproteins in crude cell lysates, 2)labeling of alkyne- or azide-tagged glycoproteins on the surface of live mammalian cells, and 3)labeling of azides in surface proteins of live Escherichia coli. Although BTTPS exhibits faster kinetics than BTTP in accelerating the CuAAC reaction in in vitro kinetic measurements, its labeling efficiency is slightly lower than BTTP in modifying biomolecules with a significant amount of negative charges due to electrostatic repulsion. Nevertheless, the negative charge conferred by the sulfate at physiological conditions significantly reduced the cellular internalization of the coordinated copper(I), thus making BTTPS-CuI a better choice for live-cell labeling.
AB - The copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC), the prototypical reaction of click chemistry, is accelerated by tris(triazolylmethyl)amine-based ligands. Herein, we compare two new ligands in this family-3-[4-({bis[(1-tert-butyl-1H-1,2,3-triazol-4-yl)methyl]amino}methyl)- 1H-1,2,3-triazol-1-yl]propanol (BTTP) and the corresponding sulfated ligand 3-[4-({bis[(1-tert-butyl-1H-1,2,3-triazol-4-yl)methyl]amino}methyl)-1H-1,2, 3-triazol-1-yl]propyl hydrogen sulfate (BTTPS)-for three bioconjugation applications: 1)labeling of alkyne-tagged glycoproteins in crude cell lysates, 2)labeling of alkyne- or azide-tagged glycoproteins on the surface of live mammalian cells, and 3)labeling of azides in surface proteins of live Escherichia coli. Although BTTPS exhibits faster kinetics than BTTP in accelerating the CuAAC reaction in in vitro kinetic measurements, its labeling efficiency is slightly lower than BTTP in modifying biomolecules with a significant amount of negative charges due to electrostatic repulsion. Nevertheless, the negative charge conferred by the sulfate at physiological conditions significantly reduced the cellular internalization of the coordinated copper(I), thus making BTTPS-CuI a better choice for live-cell labeling.
KW - bioconjugation
KW - click chemistry
KW - copper
KW - cycloaddition
KW - glycoconjugates
UR - http://www.scopus.com/inward/record.url?scp=80053464015&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=80053464015&partnerID=8YFLogxK
U2 - 10.1002/asia.201100385
DO - 10.1002/asia.201100385
M3 - Article
C2 - 21905231
AN - SCOPUS:80053464015
SN - 1861-4728
VL - 6
SP - 2796
EP - 2802
JO - Chemistry - An Asian Journal
JF - Chemistry - An Asian Journal
IS - 10
ER -