A supramolecular host–guest complex for heparin binding and sensing
نویسندگان
چکیده
منابع مشابه
Heparin sensing: blue-chip binding.
Heparin is an anionic polysaccharide that has tremendous clinical importance as an anticoagulant. Several dyes have been developed that can detect heparin, and the latest example — named Mallard Blue — has now been shown to have excellent sensing properties under biologically relevant conditions. Heparin and heparan sulfate (HS) are complex linear polysaccharides that modulate a range of normal...
متن کاملA supramolecular dissociation strategy for protein sensing.
We report a simple, robust, and general strategy for protein detection based on supramolecular dissociation. The simplicity of the design is exemplified by the fact that the host assemblies can be widely varied and that these assemblies can be achieved from commercially available surfactants. An operating mechanism that is consistent with all the data has been proposed.
متن کاملpassivity in waiting for godot and endgame: a psychoanalytic reading
this study intends to investigate samuel beckett’s waiting for godot and endgame under the lacanian psychoanalysis. it begins by explaining the most important concepts of lacanian psychoanalysis. the beckettian characters are studied regarding their state of unconscious, and not the state of consciousness as is common in most beckett studies. according to lacan, language plays the sole role in ...
Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization.
The crystal structure of a dimeric 2:2:2 FGF:FGFR:heparin ternary complex at 3 A resolution has been determined. Within each 1:1 FGF:FGFR complex, heparin makes numerous contacts with both FGF and FGFR, thereby augmenting FGF-FGFR binding. Heparin also interacts with FGFR in the adjoining 1:1 FGF:FGFR complex to promote FGFR dimerization. The 6-O-sulfate group of heparin plays a pivotal role in...
متن کاملHeparin promotes the binding of thrombin to fibrin polymer. Quantitative characterization of a thrombin-fibrin polymer-heparin ternary complex.
The binding of human alpha-thrombin (IIa) to fibrin polymer (FnIIp) was studied in the presence and absence of a high affinity 20,300 Mr heparin (H) at pH 7.4, I 0.15, and 23 degrees C. In the absence of heparin, thrombin interacts with a high affinity class of binding sites on fibrin polymer with a dissociation constant of 301 +/- 36 nM in a manner which is independent of the enzyme active sit...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nanoscale
سال: 2018
ISSN: 2040-3364,2040-3372
DOI: 10.1039/c8nr03132k