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Article: Identification of minimal peptide sequences in the (8-20) domain of human islet amyloid polypeptide involved in fibrillogenesis

TitleIdentification of minimal peptide sequences in the (8-20) domain of human islet amyloid polypeptide involved in fibrillogenesis
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date2003
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yjsbi
Citation
Journal of Structural Biology, 2003, v. 141 n. 3, p. 218-227 How to Cite?
AbstractWe have examined a series of overlapping peptide fragments from the 8-20 region of human islet amyloid polypeptide (IAPP) with the objective of defining the smallest fibril-forming domain. Peptide fragments corresponding to LANFLV (residues 12-17) and FLVHSS (residues 15-20) were strong enhancers of β-sheet transition and fibril formation. Negative stain electron microscopy illustrated the ability of these peptide fragments to form fibrils independently when incubated alone in solution. Circular dichroism analysis revealed that when full-length human IAPP was incubated in the presence of these two fragments, fibrillogenesis was accelerated. While the two fragments, LANFLV and FLVHSS, were able to enhance the recruitment of additional IAPP molecules during fibril formation, the "seeding" activity of these peptides had no effect on altering IAPP-induced cytotoxcity as determined by cell culture studies. Therefore, this study has identified two internal IAPP peptide fragments within the 8-20 domain that may have a role in enhancing the folding and aggregation of human IAPP. These fragments are the smallest sequences identified, within the 8-20 region of hIAPP, that can independently form fibrils, and that can interact with IAPP to assemble into fibrils with characteristics similar as those formed by human IAPP alone. © 2003 Elsevier Science (USA). All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/92263
ISSN
2015 Impact Factor: 2.57
2015 SCImago Journal Rankings: 3.561
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorScrocchi, LAen_HK
dc.contributor.authorHa, Ken_HK
dc.contributor.authorChen, Yen_HK
dc.contributor.authorWu, Len_HK
dc.contributor.authorWang, Fen_HK
dc.contributor.authorFraser, PEen_HK
dc.date.accessioned2010-09-17T10:40:53Z-
dc.date.available2010-09-17T10:40:53Z-
dc.date.issued2003en_HK
dc.identifier.citationJournal of Structural Biology, 2003, v. 141 n. 3, p. 218-227en_HK
dc.identifier.issn1047-8477en_HK
dc.identifier.urihttp://hdl.handle.net/10722/92263-
dc.description.abstractWe have examined a series of overlapping peptide fragments from the 8-20 region of human islet amyloid polypeptide (IAPP) with the objective of defining the smallest fibril-forming domain. Peptide fragments corresponding to LANFLV (residues 12-17) and FLVHSS (residues 15-20) were strong enhancers of β-sheet transition and fibril formation. Negative stain electron microscopy illustrated the ability of these peptide fragments to form fibrils independently when incubated alone in solution. Circular dichroism analysis revealed that when full-length human IAPP was incubated in the presence of these two fragments, fibrillogenesis was accelerated. While the two fragments, LANFLV and FLVHSS, were able to enhance the recruitment of additional IAPP molecules during fibril formation, the "seeding" activity of these peptides had no effect on altering IAPP-induced cytotoxcity as determined by cell culture studies. Therefore, this study has identified two internal IAPP peptide fragments within the 8-20 domain that may have a role in enhancing the folding and aggregation of human IAPP. These fragments are the smallest sequences identified, within the 8-20 region of hIAPP, that can independently form fibrils, and that can interact with IAPP to assemble into fibrils with characteristics similar as those formed by human IAPP alone. © 2003 Elsevier Science (USA). All rights reserved.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yjsbien_HK
dc.relation.ispartofJournal of Structural Biologyen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titleIdentification of minimal peptide sequences in the (8-20) domain of human islet amyloid polypeptide involved in fibrillogenesisen_HK
dc.typeArticleen_HK
dc.identifier.emailChen, Y:ychenc@hkucc.hku.hken_HK
dc.identifier.authorityChen, Y=rp1318en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S1047-8477(02)00630-5en_HK
dc.identifier.pmid12648568-
dc.identifier.scopuseid_2-s2.0-0037341842en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037341842&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume141en_HK
dc.identifier.issue3en_HK
dc.identifier.spage218en_HK
dc.identifier.epage227en_HK
dc.identifier.isiWOS:000181864400005-
dc.identifier.citeulike3726895-

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