Chemical modification of proteins by insertion of synthetic peptides using tandem protein trans-splicing
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Chemical modification of proteins by insertion of synthetic peptides using tandem protein trans-splicing. / Khoo, K. K.; Galleano, I.; Gasparri, F.; Wieneke, R.; Harms, H.; Poulsen, M. H.; Chua, H. C.; Wulf, M.; Tampé, R.; Pless, S. A.
In: Nature Communications, Vol. 11, No. 1, 2284, 01.12.2020.Research output: Contribution to journal › Journal article › peer-review
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TY - JOUR
T1 - Chemical modification of proteins by insertion of synthetic peptides using tandem protein trans-splicing
AU - Khoo, K. K.
AU - Galleano, I.
AU - Gasparri, F.
AU - Wieneke, R.
AU - Harms, H.
AU - Poulsen, M. H.
AU - Chua, H. C.
AU - Wulf, M.
AU - Tampé, R.
AU - Pless, S. A.
PY - 2020/12/1
Y1 - 2020/12/1
N2 - Manipulation of proteins by chemical modification is a powerful way to decipher their function. However, most ribosome-dependent and semi-synthetic methods have limitations in the number and type of modifications that can be introduced, especially in live cells. Here, we present an approach to incorporate single or multiple post-translational modifications or non-canonical amino acids into proteins expressed in eukaryotic cells. We insert synthetic peptides into GFP, NaV1.5 and P2X2 receptors via tandem protein trans-splicing using two orthogonal split intein pairs and validate our approach by investigating protein function. We anticipate the approach will overcome some drawbacks of existing protein enigineering methods.
AB - Manipulation of proteins by chemical modification is a powerful way to decipher their function. However, most ribosome-dependent and semi-synthetic methods have limitations in the number and type of modifications that can be introduced, especially in live cells. Here, we present an approach to incorporate single or multiple post-translational modifications or non-canonical amino acids into proteins expressed in eukaryotic cells. We insert synthetic peptides into GFP, NaV1.5 and P2X2 receptors via tandem protein trans-splicing using two orthogonal split intein pairs and validate our approach by investigating protein function. We anticipate the approach will overcome some drawbacks of existing protein enigineering methods.
U2 - 10.1038/s41467-020-16208-6
DO - 10.1038/s41467-020-16208-6
M3 - Journal article
C2 - 32385250
AN - SCOPUS:85084720502
VL - 11
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
IS - 1
M1 - 2284
ER -
ID: 245323680