Researchers from National Center for Nanoscience and Technology (NCNST) and Fudan University have discovered the sequence effects on peptide assemblies by using scanning tunneling microscopy (STM) and molecular dynamics (MD) simulations (J. Am. Chem. Soc., 2013, 135, 2181). The NCNST research group has been focusing on the single molecule study on peptide assembly and its modulation, and they have identified the core beta-structure motifs of the amyloid peptides by using STM in their previous works (Proc. Natl. Acad. Sci. USA, 2011, 108, 19605, etc.). These works provided a new methodology in structural analysis for non-crystalline amyloid peptides, while the sequence recognition is still very challenging because of the conformational polymorph and adsorption stability. In this work, Dr.xiaobo Mao and coauthors investigated the sequence effects on the adsorption conformation stability of the blocked polyamino acids by STM imaging and MD simulations. The sequence effects are mainly based on the consistence between the brightness contrasts in STM images and simulated interaction energy of the different residues with graphite surfaces. This work is beneficial for the understanding of the fundamental aspects in peptide interactions and assemblies.
Sequence effects on peptide assembly stability
Researchers from National Center for Nanoscience and Technology (NCNST) and Fudan University have discovered the sequence effects on peptide assemblies by using scanning tunneling microscopy (STM) and molecular dynamics (MD) simulations (J. Am. Chem. Soc., 2013, 135, 2181). The NCNST research group has been focusing on the single molecule study on peptide assembly and its modulation, and they have identified the core beta-structure motifs of the amyloid peptides by using STM in their previous works (Proc. Natl. Acad. Sci. USA, 2011, 108, 19605, etc.). These works provided a new methodology in structural analysis for non-crystalline amyloid peptides, while the sequence recognition is still very challenging because of the conformational polymorph and adsorption stability. In this work, Dr.xiaobo Mao and coauthors investigated the sequence effects on the adsorption conformation stability of the blocked polyamino acids by STM imaging and MD simulations. The sequence effects are mainly based on the consistence between the brightness contrasts in STM images and simulated interaction energy of the different residues with graphite surfaces. This work is beneficial for the understanding of the fundamental aspects in peptide interactions and assemblies.
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