Influence of alternating L-/D-amino acid chiralities and disulfide bond geometry on the capacity of cysteine-containing reversible cyclic peptides to disperse carbon nanotubes

Biopolymers ◽  
2009 ◽  
Vol 92 (3) ◽  
pp. 212-221 ◽  
Author(s):  
Eric J. Becraft ◽  
Anton S. Klimenko ◽  
Gregg R. Dieckmann
Keyword(s):  
Carbon Nanotubes ◽  
Amino Acid ◽  
Disulfide Bond ◽  
Cyclic Peptides ◽  
Disperse Carbon

scholarly journals Binding Interactions of Peptide Aptamers

Molecules ◽  
2020 ◽  
Vol 25 (24) ◽  
pp. 6055
Author(s):  
Roger R. C. New ◽  
Tam T. T. Bui ◽  
Michal Bogus
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Cyclic Peptides ◽  
Binding Interactions ◽  
Peptide Aptamers ◽  
Linear Peptide ◽  
Signalling Molecules ◽  
Antibody Binding Site ◽  
Linear Chains ◽  
Protein Receptors

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.

scholarly journals Screening for Stable Mutants with Amino Acid Pairs Substituted for the Disulfide Bond between Residues 14 and 38 of Bovine Pancreatic Trypsin Inhibitor (BPTI)

2002 ◽  
Vol 277 (52) ◽  
pp. 51043-51048 ◽  
Author(s):  
Yoshihisa Hagihara ◽  
Kentaro Shiraki ◽  
Tsutomu Nakamura ◽  
Koichi Uegaki ◽  
Masahiro Takagi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Disulfide Bond ◽  
Trypsin Inhibitor ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor

Wet Powder Metallurgy Process for Dispersing Carbon Nanotubes and Fabricating Magnesium Composite

2018 ◽  
Vol 759 ◽  
pp. 86-91 ◽  
Author(s):  
Jiang Tao Hou ◽  
Wen Bo Du ◽  
Zhao Hui Wang ◽  
Xian Du ◽  
Chao Xu
Keyword(s):  
Electron Microscopy ◽  
Carbon Nanotubes ◽  
Powder Metallurgy ◽  
Interfacial Interaction ◽  
Interface Bonding ◽  
Transmission Electron ◽  
Powder Metallurgy Process ◽  
Disperse Carbon ◽  
Effective Dispersion ◽  
Metallurgy Process

A wet powder metallurgy (WPM) process was developed to disperse carbon nanotubes (CNTs), and to fabricate the CNTs reinforced Mg matrix (CNTs/Mg) composite. The dispersion effect of CNTs were evaluated by field emission scanning electron microscopy (FE-SEM), dynamic light scattering (DLS) and high-resolution transmission electron microscopy (HR-TEM), respectively. Results showed that the CNTs were homogeneously dispersed on the surface of Mg powder. Adequate bonding and good interfacial interaction between the CNTs and Mg matrix contributed to the efficient load transferring from the CNTs to Mg matrix under a mechanical force. Furthermore, no brittle MgO was formed on the surface and it was beneficial to improving the adhesion of the CNTs to Mg matrix. With 0.5 wt.% CNTs addition, the CNTs/Mg composite experienced remarkable enhancements in tensile stress of 28% and Young’s modulus of 24%. The reasons responsible for these enhancements are suggested as the effective dispersion of the CNTs and the good interface bonding between the CNTs and Mg matrix.

Sign in / Sign up

Export Citation Format

Share Document