Staudinger Ligation: A Tool to Monitor Differential Sialic Acid Expression in Glycoproteins
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چکیده
منابع مشابه
DNA conjugation by Staudinger ligation.
Two 5 modified 2'-deoxyuridin triphosphates and a 7 modified 2'-deoxy-7-deazaadenosine were synthesized carrying a terminal azide linked to the base. For probing the sterical influence on incorporation and Staudinger ligation different sized flexible linkers were chosen. All three nucleotides can completely replace their natural counterparts in primer extension as well as polymerase chain react...
متن کاملProtein Assembly Using the Staudinger Ligation
Introduction New methods are facilitating the total chemical synthesis of proteins. In particular, the chemical ligation of synthetic peptides provides a convergent route to proteins. Currently, the most common ligation method is “native chemical ligation” [1]. In native chemical ligation, the thiolate of an N-terminal cysteine residue of one peptide attacks the C-terminal thioester of a second...
متن کاملStaudinger ligation: a peptide from a thioester and azide.
[reaction: see text] The technique of native chemical ligation enables the total chemical synthesis of proteins. This method is limited, however, by an absolute requirement for a cysteine residue at the ligation juncture. Here, this restriction is overcome with a new chemical ligation method in which a phosphinobenzenethiol is used to link a thioester and azide. The product is an amide with no ...
متن کاملStereoselective N-glycosylation by Staudinger ligation.
Stereoselective methods for the chemical synthesis of beta-N-glycosyl amides are needed to generate glycopeptides and glycoproteins. Here, we report that the Staudinger ligation can be used to form glycosylated asparagine derivatives. The reaction proceeds with high stereoselectivity, and a variety of glycosyl azides can function as substrates. Our results provide precedence for the use of this...
متن کاملSite-specific protein immobilization by Staudinger ligation.
The Staudinger ligation between an azido-protein and a phosphinothioester-derivatized surface is demonstrated to be an effective means for the site-specific, covalent immobilization of a protein. Immobilization yields of >50% are obtained in <1 min, and immobilized proteins have >80% of their expected activity. No other method enables more rapid immobilization or a higher yield of active protei...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2007
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.21.6.a998-e