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dc.contributor.authorBae, J.
dc.contributor.authorDesai, U. R.
dc.contributor.authorPervin, A.
dc.contributor.authorCaldwell, E. E.O.
dc.contributor.authorWeiler, J. M.
dc.contributor.authorLinhardt, R. J.
dc.date1994
dc.date.accessioned2022-06-27T17:14:37Z
dc.date.available2022-06-27T17:14:37Z
dc.date.issued1994-01-01
dc.identifier.citationInteraction of Heparin with Synthetic Antithrombin III Peptide Analogues, J. Bae, U.R. Desai, A. Pervin, E.O. Caldwell, J.M. Weiler, R. J. Linhardt, Biochemical Journal, 301, 121-129, 1994.
dc.identifier.issn2646021
dc.identifier.urihttps://doi.org/10.1042/bj3010121
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5967
dc.descriptionBiochemical Journal, 301, 121-129
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractHeparin-binding proteins may contain specific patterns of basic amino acids, called consensus sequences, that interact with heparin. Small peptides were synthesized that contained consensus sequences (i.e. FAKLNCRLYRKANKSSK) or disrupted consensus sequences (i.e. K136-->A) based on the known sequence of antithrombin III (amino acid residues 123-139). These peptides were then examined in both competitive and non-competitive binding experiments using bioassays, fluorescence spectroscopy, affinity chromatography and n.m.r. spectroscopy. Both the consensus and disrupted-consensus peptide bound to heparin. Peptides with consensus sequences bound specifically to the pentasaccharide antithrombin III-binding site within heparin. In contrast, peptides with disrupted consensus sequences showed no specificity, binding to any sequence within heparin. Proton nuclear Overhauser enhancement spectroscopy demonstrated the proximity of leucine and tyrosine (within the consensus sequence) to the N-acetyl moiety found primarily within the pentasaccharide antithrombin III-binding site of heparin. This experiment confirmed the findings of the other techniques and helped to localize the binding sites in both peptides and heparin. A model is proposed for both specific and non-specific heparin interaction with consensus and disrupted-consensus peptides.
dc.description.sponsorshipNational Institute of General Medical Sciences
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1042/bj3010121
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochemical Journal
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleInteraction of Heparin with Synthetic Antithrombin III Peptide Analogues
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1042/bj3010121
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dcterms.isVersionOfhttps://doi.org/10.1042/bj3010121
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages121-129
rpi.description.volume301


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