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    Self-assembling multidomain peptides tailor biological responses through biphasic release

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    Author
    Kumar, Vivek A.; Taylor, Nichole L.; Shi, Siyu; Wickremasinghe, Navindee C.; D’Souza, Rena N.; More... Hartgerink, Jeffrey D. Less...
    Date
    2015
    Abstract
    Delivery of small molecules and drugs to tissues is a mainstay of several tissue engineering strategies. Next generation treatments focused on localized drug delivery offer a more effective means in dealing with refractory healing when compared to systemic approaches. Here we describe a novel multidomain peptide hydrogel that capitalizes on synthetic peptide chemistry, supramolecular self-assembly and cytokine delivery to tailor biological responses. This material is biomimetic, shows shear stress recovery and offers a nanofibrous matrix that sequesters cytokines. The biphasic pattern of cytokine release results in the spatio-temporal activation of THP-1 monocytes and macrophages. Furthermore, macrophage–material interactions are promoted without generation of a proinflammatory environment. Subcutaneous implantation of injectable scaffolds showed a marked increase in macrophage infiltration and polarization dictated by cytokine loading as early as 3 days, with complete scaffold resorption by day 14. Macrophage interaction and response to the peptide composite facilitated the (i) recruitment of monocytes/macrophages, (ii) sustained residence of immune cells until degradation, and (iii) promotion of a pro-resolution M2 environment. Our results suggest the potential use of this injectable cytokine loaded hydrogel scaffold in a variety of tissue engineering applications.
    Citation
    Kumar, Vivek A., Taylor, Nichole L., Shi, Siyu, et al.. "Self-assembling multidomain peptides tailor biological responses through biphasic release." Biomaterials, 52, (2015) Elsevier: 71-78. https://doi.org/10.1016/j.biomaterials.2015.01.079.
    Published Version
    https://doi.org/10.1016/j.biomaterials.2015.01.079
    Keyword
    Inflammation; Macrophage polarization; Multi-domain peptide; Self-assembly
    Type
    Journal article
    Publisher
    Elsevier
    Citable link to this page
    https://hdl.handle.net/1911/94847
    Rights
    This is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Elsevier.
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    • Bioengineering Publications [632]
    • Chemistry Publications [636]
    • Faculty Publications [4988]

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    Home | FAQ | Contact Us | Privacy Notice | Accessibility Statement
    Managed by the Digital Scholarship Services at Fondren Library, Rice University
    Physical Address: 6100 Main Street, Houston, Texas 77005
    Mailing Address: MS-44, P.O.BOX 1892, Houston, Texas 77251-1892
    Site Map