Peptide-mediated synthesis of gold nanoparticles: effects of peptide sequence and nature of binding on physicochemical properties

Nanoscale ◽  
2014 ◽  
Vol 6 (6) ◽  
pp. 3165-3172 ◽  
Author(s):  
Yue Li ◽  
Zhenghua Tang ◽  
Paras N. Prasad ◽  
Marc R. Knecht ◽  
Mark T. Swihart

Size and catalytic activity of gold nanoparticles prepared using ten metal-binding peptides provide insights into peptide sequence–binding–property relationships.

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Jesica Urbina ◽  
Advait Patil ◽  
Kosuke Fujishima ◽  
Ivan G. Paulino-Lima ◽  
Chad Saltikov ◽  
...  

Abstract Electronics waste production has been fueled by economic growth and the demand for faster, more efficient consumer electronics. The glass and metals in end-of-life electronics components can be reused or recycled; however, conventional extraction methods rely on energy-intensive processes that are inefficient when applied to recycling e-waste that contains mixed materials and small amounts of metals. To make e-waste recycling economically viable and competitive with obtaining raw materials, recovery methods that lower the cost of metal reclamation and minimize environmental impact need to be developed. Microbial surface adsorption can aid in metal recovery with lower costs and energy requirements than traditional metal-extraction approaches. We introduce a novel method for metal recovery by utilizing metal-binding peptides to functionalize fungal mycelia and enhance metal recovery from aqueous solutions such as those found in bioremediation or biomining processes. Using copper-binding as a proof-of-concept, we compared binding parameters between natural motifs and those derived in silico, and found comparable binding affinity and specificity for Cu. We then combined metal-binding peptides with chitin-binding domains to functionalize a mycelium-based filter to enhance metal recovery from a Cu-rich solution. This finding suggests that engineered peptides could be used to functionalize biological surfaces to recover metals of economic interest and allow for metal recovery from metal-rich effluent with a low environmental footprint, at ambient temperatures, and under circumneutral pH.


2020 ◽  
Vol 12 (22) ◽  
pp. 24623-24634
Author(s):  
Tomonobu Kodama ◽  
Akifumi Yoshihara ◽  
Isha Goel ◽  
Masaki Sekino ◽  
Akihiro Kuwahata ◽  
...  

FEBS Letters ◽  
1986 ◽  
Vol 205 (1) ◽  
pp. 47-50 ◽  
Author(s):  
E. Grill ◽  
W. Gekeler ◽  
E.-L. Winnacker ◽  
H.H. Zenk

Biochemistry ◽  
2002 ◽  
Vol 41 (1) ◽  
pp. 343-356 ◽  
Author(s):  
Kimberly D. Copeland ◽  
Marilena P. Fitzsimons ◽  
Robert P. Houser ◽  
Jacqueline K. Barton

2005 ◽  
Vol 100 (6) ◽  
pp. 593-599 ◽  
Author(s):  
Kazumasa Hirata ◽  
Naoki Tsuji ◽  
Kazuhisa Miyamoto

Biomimetics ◽  
2019 ◽  
Vol 4 (2) ◽  
pp. 35 ◽  
Author(s):  
Nora Schönberger ◽  
Christina Zeitler ◽  
Robert Braun ◽  
Franziska L. Lederer ◽  
Sabine Matys ◽  
...  

The phage surface display technology is a useful tool to screen and to extend the spectrum of metal-binding protein structures provided by nature. The directed evolution approach allows identifying specific peptide ligands for metals that are less abundant in the biosphere. Such peptides are attractive molecules in resource technology. For example, gallium-binding peptides could be applied to recover gallium from low concentrated industrial wastewater. In this study, we investigated the affinity and selectivity of five bacteriophage clones displaying different gallium-binding peptides towards gallium and arsenic in independent biosorption experiments. The displayed peptides were highly selective towards Ga3+ whereby long linear peptides showed a lower affinity and specificity than those with a more rigid structure. Cysteine scanning was performed to determine the relationship between secondary peptide structure and gallium sorption. By site-directed mutagenesis, the amino acids of a preselected peptide sequence are systematically replaced by cysteines. The resulting disulphide bridge considerably reduces the flexibility of linear peptides. Subsequent biosorption experiments carried out with the mutants obtained from cysteine scanning demonstrated, depending on the position of the cysteines in the peptide, either a considerable increase in the affinity of gallium compared to arsenic or an increase in the affinity for arsenic compared to gallium. This study shows the impressive effect on peptide–target interaction based on peptide structure and amino acid position and composition via the newly established systematic cysteine scanning approach.


RSC Advances ◽  
2015 ◽  
Vol 5 (107) ◽  
pp. 87998-88001 ◽  
Author(s):  
Dong-Yu Tsai ◽  
Yi-Jung Tsai ◽  
Chia-Ho Yen ◽  
Chun-Yu Ouyang ◽  
Yi-Chun Yeh

Using recombinant microorganisms expressing metal binding peptides as whole-cell biocatalysts for 4-nitroaniline reduction.


1995 ◽  
Vol 270 (9) ◽  
pp. 4721-4728 ◽  
Author(s):  
Daniel F. Ortiz ◽  
Theresa Ruscitti ◽  
Kent F. McCue ◽  
David W. Ow

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