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  1. Article ; Online: Egg Case Protein 3: A Constituent of Black Widow Spider Tubuliform Silk.

    Shanafelt, Mikayla / Larracas, Camille / Dyrness, Simmone / Hekman, Ryan / La Mattina-Hawkins, Coby / Rabara, Taylor / Wu, Wilson / Vierra, Craig A

    Molecules (Basel, Switzerland)

    2021  Volume 26, Issue 16

    Abstract: Spider silk has outstanding mechanical properties, rivaling some of the best materials on the planet. Biochemical analyses of tubuliform silk have led to the identification of TuSp1, egg case protein 1, and egg case protein 2. TuSp1 belongs to the ... ...

    Abstract Spider silk has outstanding mechanical properties, rivaling some of the best materials on the planet. Biochemical analyses of tubuliform silk have led to the identification of TuSp1, egg case protein 1, and egg case protein 2. TuSp1 belongs to the spidroin superfamily, containing a non-repetitive
    MeSH term(s) Amino Acid Sequence ; Animal Structures/metabolism ; Animals ; Black Widow Spider/chemistry ; Egg Proteins/chemistry ; Egg Proteins/genetics ; Egg Proteins/metabolism ; Female ; Fibroins/chemistry ; Gene Expression Regulation ; Ovum/metabolism ; Ovum/ultrastructure ; Proteomics ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Tandem Mass Spectrometry
    Chemical Substances Egg Proteins ; RNA, Messenger ; Fibroins (9007-76-5)
    Language English
    Publishing date 2021-08-22
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules26165088
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MO 81: Show issues

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  2. Article ; Online: Comprehensive Proteomic Analysis of Spider Dragline Silk from Black Widows: A Recipe to Build Synthetic Silk Fibers.

    Larracas, Camille / Hekman, Ryan / Dyrness, Simmone / Arata, Alisa / Williams, Caroline / Crawford, Taylor / Vierra, Craig A

    International journal of molecular sciences

    2016  Volume 17, Issue 9

    Abstract: The outstanding material properties of spider dragline silk fibers have been attributed to two spidroins, major ampullate spidroins 1 and 2 (MaSp1 and MaSp2). Although dragline silk fibers have been treated with different chemical solvents to elucidate ... ...

    Abstract The outstanding material properties of spider dragline silk fibers have been attributed to two spidroins, major ampullate spidroins 1 and 2 (MaSp1 and MaSp2). Although dragline silk fibers have been treated with different chemical solvents to elucidate the relationship between protein structure and fiber mechanics, there has not been a comprehensive proteomic analysis of the major ampullate (MA) gland, its spinning dope, and dragline silk using a wide range of chaotropic agents, inorganic salts, and fluorinated alcohols to elucidate their complete molecular constituents. In these studies, we perform in-solution tryptic digestions of solubilized MA glands, spinning dope and dragline silk fibers using five different solvents, followed by nano liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) analysis with an Orbitrap Fusion™ Tribrid™. To improve protein identification, we employed three different tryptic peptide fragmentation modes, which included collision-induced dissociation (CID), electron transfer dissociation (ETD), and high energy collision dissociation (HCD) to discover proteins involved in the silk assembly pathway and silk fiber. In addition to MaSp1 and MaSp2, we confirmed the presence of a third spidroin, aciniform spidroin 1 (AcSp1), widely recognized as the major constituent of wrapping silk, as a product of dragline silk. Our findings also reveal that MA glands, spinning dope, and dragline silk contain at least seven common proteins: three members of the Cysteine-Rich Protein Family (CRP1, CRP2 and CRP4), cysteine-rich secretory protein 3 (CRISP3), fasciclin and two uncharacterized proteins. In summary, this study provides a proteomic blueprint to construct synthetic silk fibers that most closely mimic natural fibers.
    MeSH term(s) Animals ; Arthropod Proteins/chemistry ; Arthropod Proteins/isolation & purification ; Black Widow Spider/chemistry ; Black Widow Spider/metabolism ; Chromatography, Liquid ; Fibroins/chemistry ; Fibroins/isolation & purification ; Proteome/drug effects ; Proteomics/methods ; Silk/metabolism ; Solvents/pharmacology ; Tandem Mass Spectrometry
    Chemical Substances Arthropod Proteins ; Proteome ; Silk ; Solvents ; Fibroins (9007-76-5)
    Language English
    Publishing date 2016-09-13
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms17091537
    Database MEDical Literature Analysis and Retrieval System OnLINE

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