Molecular Recognition ofN-Acetylneuraminic Acid by Acyclic Pyridinium- and Quinolinium-Based Receptors in Aqueous Media: Recognition through Combination of Cationic and Neutral Recognition Sites

2012 ◽  
Vol 78 (2) ◽  
pp. 292-300 ◽  
Author(s):  
Christoph Geffert ◽  
Matthias Kuschel ◽  
Monika Mazik

Nanoscale ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 4213-4220
Author(s):  
Tatsuhiro Maekawa ◽  
Takashi Nyu ◽  
Evan Angelo Quimada Mondarte ◽  
Hiroyuki Tahara ◽  
Kasinan Suthiwanich ◽  
...  

We report a new approach to visualize the local distribution of molecular recognition sites with nanoscale resolution by amplitude-modulation atomic force microscopy.



1992 ◽  
Vol 267 (17) ◽  
pp. 12323-12329
Author(s):  
A Chattopadhyay ◽  
H.L. James ◽  
D.S. Fair


2014 ◽  
Vol 10 ◽  
pp. 1354-1364 ◽  
Author(s):  
Melanie Rauschenberg ◽  
Eva-Corrina Fritz ◽  
Christian Schulz ◽  
Tobias Kaufmann ◽  
Bart Jan Ravoo

The molecular recognition of carbohydrates and proteins mediates a wide range of physiological processes and the development of synthetic carbohydrate receptors (“synthetic lectins”) constitutes a key advance in biomedical technology. In this article we report a synthetic lectin that selectively binds to carbohydrates immobilized in a molecular monolayer. Inspired by our previous work, we prepared a fluorescently labeled synthetic lectin consisting of a cyclic dimer of the tripeptide Cys-His-Cys, which forms spontaneously by air oxidation of the monomer. Amine-tethered derivatives of N-acetylneuraminic acid (NANA), β-D-galactose, β-D-glucose and α-D-mannose were microcontact printed on epoxide-terminated self-assembled monolayers. Successive prints resulted in simple microarrays of two carbohydrates. The selectivity of the synthetic lectin was investigated by incubation on the immobilized carbohydrates. Selective binding of the synthetic lectin to immobilized NANA and β-D-galactose was observed by fluorescence microscopy. The selectivity and affinity of the synthetic lectin was screened in competition experiments. In addition, the carbohydrate binding of the synthetic lectin was compared with the carbohydrate binding of the lectins concanavalin A and peanut agglutinin. It was found that the printed carbohydrates retain their characteristic selectivity towards the synthetic and natural lectins and that the recognition of synthetic and natural lectins is strictly orthogonal.



Author(s):  
David Alsteens ◽  
Vincent Dupres ◽  
Etienne Dague ◽  
Claire Verbelen ◽  
Guillaume André ◽  
...  




2014 ◽  
Vol 71 (7) ◽  
pp. 293-301 ◽  
Author(s):  
Kazuki SAKATA ◽  
Kohei OHKUBO ◽  
Yuki HIRUTA ◽  
Eri AYANO ◽  
Hideko KANAZAWA




Biomaterials ◽  
2007 ◽  
Vol 28 (15) ◽  
pp. 2393-2402 ◽  
Author(s):  
V DUPRES ◽  
C VERBELEN ◽  
Y DUFRENE


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