(UL)
  • Structural requirements of acylated Gly-l-Ala-d-Glu analogs for activation of the innate immune receptor NOD2
    Gobec, Martina, 1983- ...
    The fragment of bacterial peptidoglycan muramyl dipeptide (MDP) has long been known for its adjuvant activity, however the underlying mechanism of this action has only recently been elucidated. It is ... ascribed to its agonist action on the nucleotide-binding oligomerization domain-containing protein 2 (NOD2). In spite of the pressing need for novel adjuvants for human use, this discovery is hampered, by not knowing the structural requirements underlying the immunostimulatory activity. We have investigated how minor modifications of hit compound acyl Gly-L-Ala-D-Glu derivative I modulate the molecular recognition by NOD2. A series of novel desmuramyldipeptides has been designed and synthesized leading to the identification of compound 16, in which the sugar moiety is replaced by a 6-phenylindole moiety, that exhibits the strongest NOD2 activation to date sans the carbohydrate moiety. The results have enabled a deeper understanding of the structural requirements of desmuramylpeptides for NOD2 activation.
    Source: European journal of medicinal chemistry. - ISSN 0223-5234 (Vol. 116, 30 Jun. 2016, str. 1-12)
    Type of material - article, component part ; adult, serious
    Publish date - 2016
    Language - english
    COBISS.SI-ID - 4041329

    Link(s):

    http://www.sciencedirect.com/science/article/pii/S0223523416302045

    Dostop preko računalnikov UL


    DOI

source: European journal of medicinal chemistry. - ISSN 0223-5234 (Vol. 116, 30 Jun. 2016, str. 1-12)

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