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. 2021 Jun 10;10(2):23. doi: 10.3390/antib10020023

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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CDR H3 of 10E8 is the cause of extended interaction with SEC. (A) Top panel, crystal structure of 10E8v4 (PDB ID:5IQ9); bottom panels, anomalous SEC profile of 10E8v4 versus antibody VRC01 control. (B) After introducing a disulfide bond by mutation of CDR H3 (Tyr100eCys) and light chain (Ser30Cys), a single peak of the 10E8v4 modified Cys100e_HC-Cys30_LC was observed, but with anomalously longer SEC profile compared to antibody VRC01. Top panel, model of the disulfide bond linked CDR H3; bottom panels, SEC chromatography of 10E8 variant highlighting anomalous SEC interaction versus antibody VRC01 control. (C) Deletion of the tip of CDR H3 (₉₉YDFWFGYPP_100g) leads to loss of extended SEC interactions. Top panel, model of the 10E8v4 structure with the tip of CDR H3 deleted; bottom panels, SEC chromatography of 10E8 variant highlighting anomalous SEC interaction versus antibody VRC01 control.