Structural Comparison between the Binding Interactions of IbpAB between Pathogenic and Non-Pathogenic Organisms: A Detailed in Sillico Approach

2020 ◽  
Author(s):  
Sangeeta Mitra ◽  
Rakhi Dasgupta ◽  
Angshuman Bagchi ◽  
Aniruddha Biswas
1997 ◽  
Vol 63 (6) ◽  
pp. 417-424 ◽  
Author(s):  
Naruto FURUYA ◽  
Shuichi YAMASAKI ◽  
Masanori NISHIOKA ◽  
Ikuo SHIRAISHI ◽  
Kazuhiro IIYAMA ◽  
...  

Author(s):  
S. Grammatikos ◽  
T. Kaimakamis ◽  
S. Panos ◽  
C. Gravalidis ◽  
A. Laskarakis ◽  
...  

Molecules ◽  
2020 ◽  
Vol 25 (24) ◽  
pp. 6055
Author(s):  
Roger R. C. New ◽  
Tam T. T. Bui ◽  
Michal Bogus

Peptide aptamers are short amino acid chains that are capable of binding specifically to ligands in the same way as their much larger counterparts, antibodies. Ligands of therapeutic interest that can be targeted are other peptide chains or loops located on the surface of protein receptors (e.g., GCPR), which take part in cell-to-cell communications either directly or via the intermediary of hormones or signalling molecules. To confer on aptamers the same sort of conformational rigidity that characterises an antibody binding site, aptamers are often constructed in the form of cyclic peptides, on the assumption that this will encourage stronger binding interactions than would occur if the aptamers were simply linear chains. However, no formal studies have been conducted to confirm the hypothesis that linear peptides will engage in stronger binding interactions with cyclic peptides than with other linear peptides. In this study, the interaction of a model cyclic decamer with a series of linear peptide constructs was compared with that of a linear peptide with the same sequence, showing that the cyclic configuration does confer benefits by increasing the strength of binding.


ACS Omega ◽  
2021 ◽  
Author(s):  
Nidhi Joshi ◽  
Deepak Kumar Tripathi ◽  
Nupur Nagar ◽  
Krishna Mohan Poluri

1968 ◽  
Vol 243 (6) ◽  
pp. 1204-1211
Author(s):  
H Kitchen ◽  
C W Easley ◽  
F W Putnam ◽  
W J Taylor

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