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Collagen adhesin–nanoparticle interaction: developing antimicrobial drugs based on the molecular structure

The pathogenic bacterial collagen‐binding protein RspB crystal structure revealed a two subdomain structure connected by a flexible linker that can “hug” the protein native substrate, collagen. In the presence of silver nanoparticles (AgNP), RspB is unable to bind to collagen.

A.S. Devi et al., Biochimica et Biophysica Acta 1820 (7), 819 (2012)
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The Rhusiopathiae surface protein B (RspB) is a bacterial collagen‐binding protein crucial for pathogenic bacteria colonization. The structural insight gained from this work suggest that RspB binds collagen by a unique ligand binding mechanism called “Collagen Hug”. Interaction studies between RspB and silver nanoparticles, using complementary molecular biology tecniques, show that the “Collagen Hug” mechanism is inhibited in the presence of 10 nm silver nanoparticles (AgNP).
Crystal structure information suggests that this is due to the formation of RspB protein corona tightly bonded to the AgNPs.
 

With the rapid rise in antibiotic resistance, designing alternative strategies to reduce/eliminate bacterial colonization is absolutely essential: details of this inhibition mechanism are useful for the development of antimicrobial materials and antiadhesion drugs.


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Collagen adhesin–nanoparticle interaction impairs adhesin's ligand binding mechanism; A. S. Devi, Y. Ogawa, Y. Shimoji, S. Balakumar, K. Ponnuraj, Biochimica et Biophysica Acta 1820 (7), 819 (2012)
doi: 10.1016/j.bbagen.2012.04.006.

Last Updated on Monday, 11 January 2016 15:36