Harnessing a catalytic lysine residue for the one-step preparation of homogeneous antibody-drug conjugates
Current strategies for producing antibody-drug conjugates often rely on inefficient conjugation chemistry or on generating mutations in the antibody sequence. Here the authors demonstrate a mutation-free, single-step conjugation platform utilizing a buried lysine residue.
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2017-10-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-017-01257-1 |
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doaj-327d54533f8140538f895070e14be5c52021-05-11T07:02:39ZengNature Publishing GroupNature Communications2041-17232017-10-01811910.1038/s41467-017-01257-1Harnessing a catalytic lysine residue for the one-step preparation of homogeneous antibody-drug conjugatesAlex R. Nanna0Xiuling Li1Even Walseng2Lee Pedzisa3Rebecca S. Goydel4David Hymel5Terrence R. Burke Jr.6William R. Roush7Christoph Rader8Department of Immunology and Microbiology, The Scripps Research InstituteDepartment of Immunology and Microbiology, The Scripps Research InstituteDepartment of Immunology and Microbiology, The Scripps Research InstituteDepartment of Chemistry, The Scripps Research InstituteDepartment of Immunology and Microbiology, The Scripps Research InstituteChemical Biology Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of HealthChemical Biology Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of HealthDepartment of Chemistry, The Scripps Research InstituteDepartment of Immunology and Microbiology, The Scripps Research InstituteCurrent strategies for producing antibody-drug conjugates often rely on inefficient conjugation chemistry or on generating mutations in the antibody sequence. Here the authors demonstrate a mutation-free, single-step conjugation platform utilizing a buried lysine residue.https://doi.org/10.1038/s41467-017-01257-1 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Alex R. Nanna Xiuling Li Even Walseng Lee Pedzisa Rebecca S. Goydel David Hymel Terrence R. Burke Jr. William R. Roush Christoph Rader |
spellingShingle |
Alex R. Nanna Xiuling Li Even Walseng Lee Pedzisa Rebecca S. Goydel David Hymel Terrence R. Burke Jr. William R. Roush Christoph Rader Harnessing a catalytic lysine residue for the one-step preparation of homogeneous antibody-drug conjugates Nature Communications |
author_facet |
Alex R. Nanna Xiuling Li Even Walseng Lee Pedzisa Rebecca S. Goydel David Hymel Terrence R. Burke Jr. William R. Roush Christoph Rader |
author_sort |
Alex R. Nanna |
title |
Harnessing a catalytic lysine residue for the one-step preparation of homogeneous antibody-drug conjugates |
title_short |
Harnessing a catalytic lysine residue for the one-step preparation of homogeneous antibody-drug conjugates |
title_full |
Harnessing a catalytic lysine residue for the one-step preparation of homogeneous antibody-drug conjugates |
title_fullStr |
Harnessing a catalytic lysine residue for the one-step preparation of homogeneous antibody-drug conjugates |
title_full_unstemmed |
Harnessing a catalytic lysine residue for the one-step preparation of homogeneous antibody-drug conjugates |
title_sort |
harnessing a catalytic lysine residue for the one-step preparation of homogeneous antibody-drug conjugates |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2017-10-01 |
description |
Current strategies for producing antibody-drug conjugates often rely on inefficient conjugation chemistry or on generating mutations in the antibody sequence. Here the authors demonstrate a mutation-free, single-step conjugation platform utilizing a buried lysine residue. |
url |
https://doi.org/10.1038/s41467-017-01257-1 |
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