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dc.contributor.authorNi, Guoying
dc.contributor.authorWang, Yuejian
dc.contributor.authorCummins, Scott
dc.contributor.authorWalton, Shelley
dc.contributor.authorMounsey, Kate
dc.contributor.authorLiu, Xiaosong
dc.contributor.authorWei, Ming Q
dc.contributor.authorWang, Tianfang
dc.date.accessioned2018-09-11T03:53:31Z
dc.date.available2018-09-11T03:53:31Z
dc.date.issued2017
dc.identifier.issn2164-5515
dc.identifier.doi10.1080/21645515.2016.1238537
dc.identifier.urihttp://hdl.handle.net/10072/143164
dc.description.abstractInterleukin 10 (IL-10) is a cytokine that is able to downregulate inflammation. Its overexpression is directly associated with the difficulty in the clearance of chronic viral infections, such as chronic hepatitis B, hepatitis C and HIV infection, and infection-related cancer. IL-10 signaling blockade has been proposed as a promising way of clearing chronic viral infection and preventing tumor growth in animal models. Recently, we have reported that peptides with a helical repeating pattern of hydrophobic and hydrophilic residues are able to inhibit IL-10 significantly both in vitro and in vivo. In this work, we seek to further study the inhibiting mechanism of these peptides using sequence-modified peptides. As evidenced by both experimental and molecular dynamics simulation in concert the N-terminal hydrophobic peptide constructed with repeating hydrophobic and hydrophilic pattern of residues is more likely to inhibit IL10. In addition, the sequence length and the ability of protonation are also important for inhibition activity.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherTaylor & Francis
dc.relation.ispartofpagefrom1
dc.relation.ispartofpageto32
dc.relation.ispartofjournalHuman Vaccines & Immunotherapeutics
dc.subject.fieldofresearchImmunology
dc.subject.fieldofresearchMedical microbiology
dc.subject.fieldofresearchMedical microbiology not elsewhere classified
dc.subject.fieldofresearchPharmacology and pharmaceutical sciences
dc.subject.fieldofresearchcode3204
dc.subject.fieldofresearchcode3207
dc.subject.fieldofresearchcode320799
dc.subject.fieldofresearchcode3214
dc.titleInhibitory mechanism of peptides with a repeating hydrophobic and hydrophilic residue pattern on interleukin-10
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.facultyGriffith Health, School of Medical Science
gro.description.notepublicThis publication has been entered into Griffith Research Online as an Advanced Online Version.
gro.hasfulltextNo Full Text
gro.griffith.authorWei, Ming Q.
gro.griffith.authorNi, Guoying


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