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Article: DNA-directed formation of peptide bond: A model study toward DNA-programmed peptide ligation

TitleDNA-directed formation of peptide bond: A model study toward DNA-programmed peptide ligation
Authors
Issue Date2012
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/tet
Citation
Tetrahedron, 2012, v. 68 n. 26, p. 5152-5156 How to Cite?
AbstractA model study of DNA-directed peptide ligation has been developed by transferring fluorescent reporting group from small molecule thioester to a DNA strand (template DNA) in the presence of a thiol-functionalized DNA strand (auxiliary DNA), mimicking the Native Chemical Ligation (NCL) reaction. This DNA-directed transfer shows dependence on the sequence complementarity of the two DNA strands, with in situ generated 4-thiolphenylmethyl functionalized oligonucleotide as the auxiliary DNA strand, under mild basic condition (pH=8.5), and with tris(2-carboxyethyl) phosphine hydrochloride (TCEP) as a reducing agent. Reactions with different amino acid α-thioesters resulted in varied transfer efficiencies from glycine to α-substituted amino acids. This study has provided the basic foundation to use DNA-programmed chemistry toward the chemical synthesis or unnatural modification of protein molecules. © 2012 Published by Elsevier Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/221122
ISSN
2015 Impact Factor: 2.645
2015 SCImago Journal Rankings: 0.991
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorZhang, C-
dc.contributor.authorLi, Y-
dc.contributor.authorZhang, M-
dc.contributor.authorLi, X-
dc.date.accessioned2015-10-27T09:34:04Z-
dc.date.available2015-10-27T09:34:04Z-
dc.date.issued2012-
dc.identifier.citationTetrahedron, 2012, v. 68 n. 26, p. 5152-5156-
dc.identifier.issn0040-4020-
dc.identifier.urihttp://hdl.handle.net/10722/221122-
dc.description.abstractA model study of DNA-directed peptide ligation has been developed by transferring fluorescent reporting group from small molecule thioester to a DNA strand (template DNA) in the presence of a thiol-functionalized DNA strand (auxiliary DNA), mimicking the Native Chemical Ligation (NCL) reaction. This DNA-directed transfer shows dependence on the sequence complementarity of the two DNA strands, with in situ generated 4-thiolphenylmethyl functionalized oligonucleotide as the auxiliary DNA strand, under mild basic condition (pH=8.5), and with tris(2-carboxyethyl) phosphine hydrochloride (TCEP) as a reducing agent. Reactions with different amino acid α-thioesters resulted in varied transfer efficiencies from glycine to α-substituted amino acids. This study has provided the basic foundation to use DNA-programmed chemistry toward the chemical synthesis or unnatural modification of protein molecules. © 2012 Published by Elsevier Ltd.-
dc.languageeng-
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/tet-
dc.relation.ispartofTetrahedron-
dc.rights© <year>. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/-
dc.titleDNA-directed formation of peptide bond: A model study toward DNA-programmed peptide ligation-
dc.typeArticle-
dc.identifier.emailLi, X: xiaoyuli@hku.hk-
dc.identifier.authorityLi, X=rp02080-
dc.identifier.doi10.1016/j.tet.2012.04.032-
dc.identifier.scopuseid_2-s2.0-84861684664-
dc.identifier.volume68-
dc.identifier.issue26-
dc.identifier.spage5152-
dc.identifier.epage5156-
dc.identifier.isiWOS:000305381700005-
dc.publisher.placeUnited Kingdom-

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