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dc.contributor.authorCaldwell, E.E.O.
dc.contributor.authorNadkarni, V.D.
dc.contributor.authorFromm, J.R.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorWeiler, J.M.
dc.date1996
dc.date.accessioned2022-06-27T17:13:46Z
dc.date.available2022-06-27T17:13:46Z
dc.date.issued1996
dc.identifier.citationImportance of Basic Amino Acids in Heparin and Heparan Sulfate Protein Binding Sites, E. E. O. Caldwell, V. D. Nadkarni, J. R. Fromm, R.J. Linhardt, J. M. Weiler International Journal of Biochemistry and Cell Biology, 28, 203-216, 1996.
dc.identifier.urihttps://doi.org/10.1016/1357-2725(95)00123-9
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5940
dc.descriptionInternational Journal of Biochemistry and Cell Biology, 28, 203-216
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 and heparan sulfate bind a variety of proteins and peptides to regulate many biological activities. Past studies have examined a limited number of established heparin binding sites and have focused on basic amino acids when modeling binding site structural motifs. This study examines the prevalence of individual amino acids in peptides binding to heparin or heparan sulfate. A 7-mer random peptide library was synthesized using the 20 common amino acids. This 7-mer library was affinity separated using both heparin and heparan sulfate-Sepharose. Bound peptide populations were eluted with a salt step gradient (pH 7) and analysed for amino acid composition. Peptides released from heparin-Sepharose by 0.3 M NaCl were enriched in arginine, lysine, glycine and serine; and depleted in methionine and phenylalanine. In contrast, peptides released from heparan sulfate-Sepharose were enriched in arginine, glycine, serine, and proline (at 0.15 M NaCl). These peptides were depleted in histidine, isoleucine, methionine (not detectable) and phenylalanine. In the heparin binding sites of proteins, which have been published, the enriched amino acids were arginine, lysine and tyrosine. Depleted amino acids include aspartic acid, glutamic acid, glutamine, alanine, glycine, phenylalanine, serine, threonine and valine. This study demonstrates that heparin and heparan sulfate bind different populations of peptide sequences. The differences in amino acid composition indicate that the positive charge density and spacing requirements differ for peptides binding these two glycosaminoglycans.
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/1357-2725(95)00123-9
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleImportance of Basic Amino Acids in Heparin and Heparan Sulfate Protein Binding Sites
dc.typeArticle
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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)


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