DataSheet1_Low Molar Mass Dextran: One-Step Synthesis With Dextransucrase by Site-Directed Mutagenesis and its Potential of Iron-Loading.docx
Iron dextran is a common anti-anemia drug, and it requires low molar mass dextran as substrate. In this work, we selected 11 amino acid residues in domain A/B of DSR-MΔ2 within a 5-angstrom distance from sucrose for site-directed mutagenesis by molecular docking. Mutation of Q634 did not affect the enzyme catalytic activity, but showed an obvious impact on the ratio of low molecular weight dextran (L-dextran, 3,000–5,000 Da) and relatively higher molecular weight dextran (H-dextran, around 10,000 Da). L-dextran was the main product synthesized by DSR-MΔ2 Q634A, and its average molecular weight was 3,951 Da with a polydispersity index <1.3. The structural characterization of this homopolysaccharide revealed that it was a dextran, with 86.0% α(1→6) and 14.0% α(1→4) glycosidic linkages. Moreover, L-dextran was oxidized with NaOH and chelated with ferric trichloride, and an OL-dextran-iron complex was synthesized with a high iron-loading potential of 33.5% (w/w). Altogether, mutation of amino acids near the sucrose binding site of dextransucrase can affect the chain elongation process, making it possible to modulate dextran size.
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References
- https://doi.org//10.3389/fbioe.2015.00200
- https://doi.org//10.1016/j.ijbiomac.2013.04.046
- https://doi.org//10.1016/j.ijbiomac.2012.09.014
- https://doi.org//10.1016/j.carbpol.2010.07.024
- https://doi.org//10.1016/j.ijbiomac.2019.11.151
- https://doi.org//10.1039/c7nj04341d
- https://doi.org//10.1016/j.ijbiomac.2019.10.041
- https://doi.org//10.1021/acs.biochem.9b00373
- https://doi.org//10.1021/acscatal.7b02182
- https://doi.org//10.3389/fbioe.2021.691528
- https://doi.org//10.1016/j.carbpol.2014.06.018
- https://doi.org//10.1016/j.carbpol.2018.02.075
- https://doi.org//10.1016/j.jmb.2011.02.028
- https://doi.org//10.1016/j.ejpb.2011.03.016
- https://doi.org//10.1097/MNH.0000000000000263
- https://doi.org//10.3109/10242422.2012.676301
- https://doi.org//10.1016/j.jbiotec.2012.06.037
- https://doi.org//10.1016/j.chemosphere.2016.06.010
- https://doi.org//10.1155/2019/6416941
- https://doi.org//10.1016/j.carbpol.2008.07.014
- https://doi.org//10.1016/j.foodhyd.2013.10.014
- https://doi.org//10.1016/j.foodchem.2016.12.015
- https://doi.org//10.1016/j.carbpol.2017.02.030
- https://doi.org//10.1074/jbc.m604850200
- https://doi.org//10.3109/09637486.2012.734289
- https://doi.org//10.1016/j.ijbiomac.2017.10.048
- https://doi.org//10.1016/j.ijbiomac.2013.06.001
- https://doi.org//10.1107/S1744309106024729
- https://doi.org//10.1073/pnas.1007531107
- https://doi.org//10.1186/s12934-020-01361-w
- https://doi.org//10.1007/s10118-021-2506-2
- https://doi.org//10.1128/AEM.02810-17
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