Cargando…
A de novo protein catalyzes the synthesis of semiconductor quantum dots
De novo proteins constructed from novel amino acid sequences are distinct from proteins that evolved in nature. Construct K (ConK) is a binary-patterned de novo designed protein that rescues Escherichia coli from otherwise toxic concentrations of copper. ConK was recently found to bind the cofactor...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9907092/ https://www.ncbi.nlm.nih.gov/pubmed/36508665 http://dx.doi.org/10.1073/pnas.2204050119 |
_version_ | 1784884102102515712 |
---|---|
author | Spangler, Leah C. Yao, Yueyu Cheng, Guangming Yao, Nan Chari, Sarangan L. Scholes, Gregory D. Hecht, Michael H. |
author_facet | Spangler, Leah C. Yao, Yueyu Cheng, Guangming Yao, Nan Chari, Sarangan L. Scholes, Gregory D. Hecht, Michael H. |
author_sort | Spangler, Leah C. |
collection | PubMed |
description | De novo proteins constructed from novel amino acid sequences are distinct from proteins that evolved in nature. Construct K (ConK) is a binary-patterned de novo designed protein that rescues Escherichia coli from otherwise toxic concentrations of copper. ConK was recently found to bind the cofactor PLP (pyridoxal phosphate, the active form of vitamin B(6)). Here, we show that ConK catalyzes the desulfurization of cysteine to H(2)S, which can be used to synthesize CdS nanocrystals in solution. The CdS nanocrystals are approximately 3 nm, as measured by transmission electron microscope, with optical properties similar to those seen in chemically synthesized quantum dots. The CdS nanocrystals synthesized using ConK have slower growth rates and a different growth mechanism than those synthesized using natural biomineralization pathways. The slower growth rate yields CdS nanocrystals with two desirable properties not observed during biomineralization using natural proteins. First, CdS nanocrystals are predominantly of the zinc blende crystal phase; this is in stark contrast to natural biomineralization routes that produce a mixture of zinc blende and wurtzite phase CdS. Second, in contrast to the growth and eventual precipitation observed in natural biomineralization systems, the CdS nanocrystals produced by ConK stabilize at a final size. Future optimization of CdS nanocrystal growth using ConK—or other de novo proteins—may help to overcome the limits on nanocrystal quality typically observed from natural biomineralization by enabling the synthesis of more stable, high-quality quantum dots at room temperature. |
format | Online Article Text |
id | pubmed-9907092 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | National Academy of Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-99070922023-06-12 A de novo protein catalyzes the synthesis of semiconductor quantum dots Spangler, Leah C. Yao, Yueyu Cheng, Guangming Yao, Nan Chari, Sarangan L. Scholes, Gregory D. Hecht, Michael H. Proc Natl Acad Sci U S A Biological Sciences De novo proteins constructed from novel amino acid sequences are distinct from proteins that evolved in nature. Construct K (ConK) is a binary-patterned de novo designed protein that rescues Escherichia coli from otherwise toxic concentrations of copper. ConK was recently found to bind the cofactor PLP (pyridoxal phosphate, the active form of vitamin B(6)). Here, we show that ConK catalyzes the desulfurization of cysteine to H(2)S, which can be used to synthesize CdS nanocrystals in solution. The CdS nanocrystals are approximately 3 nm, as measured by transmission electron microscope, with optical properties similar to those seen in chemically synthesized quantum dots. The CdS nanocrystals synthesized using ConK have slower growth rates and a different growth mechanism than those synthesized using natural biomineralization pathways. The slower growth rate yields CdS nanocrystals with two desirable properties not observed during biomineralization using natural proteins. First, CdS nanocrystals are predominantly of the zinc blende crystal phase; this is in stark contrast to natural biomineralization routes that produce a mixture of zinc blende and wurtzite phase CdS. Second, in contrast to the growth and eventual precipitation observed in natural biomineralization systems, the CdS nanocrystals produced by ConK stabilize at a final size. Future optimization of CdS nanocrystal growth using ConK—or other de novo proteins—may help to overcome the limits on nanocrystal quality typically observed from natural biomineralization by enabling the synthesis of more stable, high-quality quantum dots at room temperature. National Academy of Sciences 2022-12-12 2022-12-20 /pmc/articles/PMC9907092/ /pubmed/36508665 http://dx.doi.org/10.1073/pnas.2204050119 Text en Copyright © 2022 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by-nc-nd/4.0/This article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Biological Sciences Spangler, Leah C. Yao, Yueyu Cheng, Guangming Yao, Nan Chari, Sarangan L. Scholes, Gregory D. Hecht, Michael H. A de novo protein catalyzes the synthesis of semiconductor quantum dots |
title | A de novo protein catalyzes the synthesis of semiconductor quantum dots |
title_full | A de novo protein catalyzes the synthesis of semiconductor quantum dots |
title_fullStr | A de novo protein catalyzes the synthesis of semiconductor quantum dots |
title_full_unstemmed | A de novo protein catalyzes the synthesis of semiconductor quantum dots |
title_short | A de novo protein catalyzes the synthesis of semiconductor quantum dots |
title_sort | de novo protein catalyzes the synthesis of semiconductor quantum dots |
topic | Biological Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9907092/ https://www.ncbi.nlm.nih.gov/pubmed/36508665 http://dx.doi.org/10.1073/pnas.2204050119 |
work_keys_str_mv | AT spanglerleahc adenovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT yaoyueyu adenovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT chengguangming adenovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT yaonan adenovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT charisaranganl adenovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT scholesgregoryd adenovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT hechtmichaelh adenovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT spanglerleahc denovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT yaoyueyu denovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT chengguangming denovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT yaonan denovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT charisaranganl denovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT scholesgregoryd denovoproteincatalyzesthesynthesisofsemiconductorquantumdots AT hechtmichaelh denovoproteincatalyzesthesynthesisofsemiconductorquantumdots |