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    Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/7297


    Title: Enzymatic stability and immunoregulatory efficacy of a synthetic indolicidin analogue with regular enantiomeric sequence
    Authors: Chang, CY;Lin, CW;Chiang, SK;Chen, PL;Huang, CY;Liu, SJ;Chong, P;Huang, MH
    Contributors: Division of Vaccine Research and Development
    Abstract: Cell-mediated immunity plays a major role in protecting the host from viral infections and tumor challenge. Here, we report the enzymatic stability and adjuvanticity of a peptiomimetic stereoisomer of the bovine neutrophil peptide indolicidin. The analogue, dubbed LD-indolicidin, contains the regular enantiomeric sequence of indolicidin and is synthesized by general stepwise solid-phase strategy. LD-Indolicidin possesses high resistance to enzymatic degradation and shows tolerance in mice. As vaccine adjuvant, LD-indolicidin is better able than the native form of indolicidin to enhance cell-mediated immune responses, using inactivated H5N1 virus as a model antigen. Taken together, these results open up a new approach to the development of vaccine adjuvants and immunotherapy technologies.
    Date: 2013-06-13
    Relation: ACS Medicinal Chemistry Letters. 2013 Jun 13;4(6):522-526.
    Link to: http://dx.doi.org/10.1021/ml400081f
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=1948-5875&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000321883900008
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84879079732
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