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    Chemobiocatalytic Synthesis of a Low Molecular Weight Heparin

    Author
    Yu, Yanlei; Fu, Li; He, Peng; Xia, Ke; Varghese, Sony; Wang, Hong; Zhang, Fuming; Dordick, Jonathan; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    Other Contributors
    Date Issued
    2022-03-18
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
    Full Citation
    Chemobiocatalytic Synthesis of a Low Molecular Weight Heparin, Y. Yu, L. Fu, P. He, K. Xia, S. Varghese, H. Wang, F. Zhang, J. Dordick, R.J. Linhardt, ACS Chemical Biology,17, 637-646, 2022.
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    URI
    https://doi.org/10.1021/acschembio.1c00928; https://hdl.handle.net/20.500.13015/5428
    Abstract
    Heparin products are widely used clinical anticoagulants essential in the practice of modern medicine. Low-molecular-weight heparins (LMWHs) are currently prepared by the controlled chemical or enzymatic depolymerization of unfractionated heparins (UFHs) that are extracted from animal tissues. In many clinical applications, LMWHs have displaced UFHs and currently comprise over 60% of the heparin market. In the past, our laboratory has made extensive efforts to prepare bioengineered UFHs relying on a chemoenzymatic process to address concerns about animal-sourced UFHs. The current study describes the use of a novel chemoenzymatic process to prepare a chemobiosynthetic LMWH from a low-molecular-weight heparosan. The resulting chemobiocatalytic LMWH matches most of the United States pharmacopeial specifications for enoxaparin, a LMWH prepared through the base-catalyzed depolymerization of animal-derived UFH.;
    Description
    ACS Chemical Biology,17, 637-646; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; ACS Chemical Biology; https://harc.rpi.edu/;
    Access
    https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/acschembio.1c00928;
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