Conjugating Hemoglobin and Albumin by Strain-Promoted Azide- Alkyne Cycloaddition.

Autor: Lee C; Davenport Chemistry Laboratories, Department of Chemistry, University of Toronto, Toronto, Ontario, M5S 3H6, Canada., Chung HW; Davenport Chemistry Laboratories, Department of Chemistry, University of Toronto, Toronto, Ontario, M5S 3H6, Canada., Kluger R; Davenport Chemistry Laboratories, Department of Chemistry, University of Toronto, Toronto, Ontario, M5S 3H6, Canada.
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Aug 19; Vol. 25 (16), pp. e202400206. Date of Electronic Publication: 2024 Jul 22.
DOI: 10.1002/cbic.202400206
Abstrakt: A one-to-one conjugate of cross-linked human hemoglobin and human serum albumin results from a strain-promoted alkyne-azide cycloaddition (SPAAC) of the modified proteins. Additions of a strained alkyne-substituted maleimide to the Cys-34 thiol of human serum albumin and an azide-containing cross-link between the amino groups of each β-unit at Lys-82 of human hemoglobin provide sites for coupling by the SPAAC process. The coupled hemoglobin-albumin conjugate can be readily purified from unreacted hemoglobin. The oxygen binding properties of the two-protein bioconjugate demonstrate oxygen affinity and cooperativity that are suitable for use in an acellular oxygen carrier.
(© 2024 The Authors. ChemBioChem published by Wiley-VCH GmbH.)
Databáze: MEDLINE
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