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  1. Article ; Online: Structure-guided identification of a peptide for bio-enabled gold nanoparticle synthesis.

    Thaker, Amar / Sirajudeen, Luqmanal / Simmons, Chad R / Nannenga, Brent L

    Biotechnology and bioengineering

    2021  Volume 118, Issue 12, Page(s) 4867–4873

    Abstract: In this study, we show that maltose-binding protein (MBP) is capable of facilitating stable gold nanoparticle synthesis, and a structure of MBP in the presence of gold ions was determined by X-ray crystallography. Using this high-resolution structure of ... ...

    Abstract In this study, we show that maltose-binding protein (MBP) is capable of facilitating stable gold nanoparticle synthesis, and a structure of MBP in the presence of gold ions was determined by X-ray crystallography. Using this high-resolution structure of gold ion bound MBP, a peptide (AT1) was selected and synthesized and was shown to also aid in the synthesis of stable gold nanoparticles under similar experimental conditions to those used for protein facilitated synthesis. This structure-based approach represents a new potential method for the selection of peptides capable of facilitating stable nanoparticle synthesis.
    MeSH term(s) Biomineralization ; Biotechnology/methods ; Crystallography ; Escherichia coli/metabolism ; Gold/chemistry ; Gold/metabolism ; Metal Nanoparticles/chemistry ; Nanotechnology/methods ; Peptides/chemistry
    Chemical Substances Peptides ; Gold (7440-57-5)
    Language English
    Publishing date 2021-09-06
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 280318-5
    ISSN 1097-0290 ; 0006-3592
    ISSN (online) 1097-0290
    ISSN 0006-3592
    DOI 10.1002/bit.27927
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: Protein-Nanoparticle Complex Structure Determination by Cryo-Electron Microscopy.

    Sen, Sagnik / Thaker, Amar / Sirajudeen, Luqmanal / Williams, Dewight / Nannenga, Brent L

    ACS applied bio materials

    2022  

    Abstract: Methods that allow the study of the structure of proteins in complex with nanomaterials promise to enhance our understanding of how biological molecules interface with inorganic materials. We used single-particle cryo-electron microscopy (cryo-EM) to ... ...

    Abstract Methods that allow the study of the structure of proteins in complex with nanomaterials promise to enhance our understanding of how biological molecules interface with inorganic materials. We used single-particle cryo-electron microscopy (cryo-EM) to demonstrate the potential for cryo-EM analysis to reveal structural details of protein-nanoparticle complexes. Two protein-nanomaterial complexes, namely, GroEL bound to platinum nanoparticles (GroEL-PtNP) and ferritin bound to an iron oxide nanoparticle, were used as model samples. For the GroEL-PtNP complex, a final reconstruction was obtained to 3.93 Å, which allowed us to fit the atomic model of GroEL into the resulting map. This sets the stage for future work and improvements on the use of cryo-EM for the study of protein-nanomaterial complexes.
    Language English
    Publishing date 2022-05-19
    Publishing country United States
    Document type Journal Article
    ISSN 2576-6422
    ISSN (online) 2576-6422
    DOI 10.1021/acsabm.2c00130
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Beam-sensitive metal-organic framework structure determination by microcrystal electron diffraction.

    Banihashemi, Fateme / Bu, Guanhong / Thaker, Amar / Williams, Dewight / Lin, Jerry Y S / Nannenga, Brent L

    Ultramicroscopy

    2020  Volume 216, Page(s) 113048

    Abstract: Analysis of metal-organic framework (MOF) structure by electron microscopy and electron diffraction offers an alternative to growing large single crystals for high-resolution X-ray diffraction. However, many MOFs are electron beam-sensitive, which can ... ...

    Abstract Analysis of metal-organic framework (MOF) structure by electron microscopy and electron diffraction offers an alternative to growing large single crystals for high-resolution X-ray diffraction. However, many MOFs are electron beam-sensitive, which can make structural analysis using high-resolution electron microscopy difficult. In this work we use the microcrystal electron diffraction (MicroED) method to collect high-resolution electron diffraction data from a model beam-sensitive MOF, ZIF-8. The diffraction data could be used to determine the structure of ZIF-8 to 0.87 Å from a single ZIF-8 nanocrystal, and this refined structure compares well with previously published structures of ZIF-8 determined by X-ray crystallography. This demonstrates that MicroED can be a valuable tool for the analysis of beam-sensitive MOF structures directly from nano and microcrystalline material.
    Language English
    Publishing date 2020-06-10
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1479043-9
    ISSN 1879-2723 ; 0304-3991
    ISSN (online) 1879-2723
    ISSN 0304-3991
    DOI 10.1016/j.ultramic.2020.113048
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Protein-facilitated gold nanoparticle formation as indicators of ionizing radiation.

    Thaker, Amar / Pushpavanam, Karthik / Bista, Tomasz / Sapareto, Stephen / Rege, Kaushal / Nannenga, Brent L

    Biotechnology and bioengineering

    2019  Volume 116, Issue 12, Page(s) 3160–3167

    Abstract: The use of X-ray radiation in radiotherapy is a common treatment for many cancers. Despite several scientific advances, determination of radiation delivered to the patient remains a challenge due to the inherent limitations of existing dosimeters ... ...

    Abstract The use of X-ray radiation in radiotherapy is a common treatment for many cancers. Despite several scientific advances, determination of radiation delivered to the patient remains a challenge due to the inherent limitations of existing dosimeters including fabrication and operation. Here, we describe a colorimetric nanosensor that exhibits unique changes in color as a function of therapeutically relevant radiation dose (3-15 Gy). The nanosensor is formulated using a gold salt and maltose-binding protein as a templating agent, which upon exposure to ionizing radiation is converted to gold nanoparticles. The formation of gold nanoparticles from colorless precursor salts renders a change in color that can be observed visually. The dose-dependent multicolored response was quantified through a simple ultraviolet-visible spectrophotometer and the peak shift associated with the different colored dispersions was used as a quantitative indicator of therapeutically relevant radiation doses. The ease of fabrication, visual color changes upon exposure to ionizing radiation, and quantitative read-out demonstrates the potential of protein-facilitated biomineralization approaches to promote the development of next-generation detectors for ionizing radiation.
    MeSH term(s) Escherichia coli/chemistry ; Escherichia coli Proteins/chemistry ; Gamma Rays ; Gold/chemistry ; Metal Nanoparticles/chemistry ; Periplasmic Binding Proteins/chemistry
    Chemical Substances Escherichia coli Proteins ; MalE protein, E coli ; Periplasmic Binding Proteins ; Gold (7440-57-5)
    Language English
    Publishing date 2019-09-23
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 280318-5
    ISSN 1097-0290 ; 0006-3592
    ISSN (online) 1097-0290
    ISSN 0006-3592
    DOI 10.1002/bit.27163
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 960: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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