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Hwang, Jae Sam; Lee, Jin Sung; Goo, Tae Won; Yun, Eun Young; Lee, Kwang-Sik; Kim, Yong‐Sung; Jin, Byung Rae; Lee, Sang Mong; Kim, Keun Young; Kang, Seok Woo; Suh, Dong Sang

doi:10.1023/a:1010542011150

Cited by 38 publications

(26 citation statements)

References 11 publications

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“…1). This composition resembles the 43% alanine, 27% glycine, and 11% serine of the H-fibroin of the saturniid silkmoths, A. yamamai and A. pernyi (Sezutsu and Yukuhiro 2000; Hwang et al 2001). In other moth H-fibroins, alanine is typically much lower (e.g., 26% in the H-fibroin of Y. evonymellus ; Yonemura and Sehnal 2006).…”

Section: Resultsmentioning

confidence: 78%

Molecular Evolution of Lepidopteran Silk Proteins: Insights from the Ghost Moth, Hepialus californicus

et al. 2010

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Silk production has independently evolved in numerous arthropod lineages, such as Lepidoptera, the moths and butterflies. Lepidopteran larvae (caterpillars) synthesize silk proteins in modified salivary glands and spin silk fibers into protective tunnels, escape lines, and pupation cocoons. Molecular sequence data for these proteins are necessary to determine critical features of their function and evolution. To this end, we constructed an expression library from the silk glands of the ghost moth, Hepialus californicus, and characterized light chainfibroin and heavy chain fibroin gene transcripts. The predicted H. californicus silk fibroins share many elements with other lepidopteran and trichopteran fibroins, such as conserved placements of cysteine, aromatic, and polar amino acid residues. Further comparative analyses were performed to determine site-specific signatures of selection and to assess whether fibroin genes are informative as phylogenetic markers. We found that purifying selection has constrained mutation within the fibroins and that light chain fibroin is a promising molecular marker. Thus, by characterizing the H. californicus fibroins, we identified key functional amino acids and gained insight into the evolutionary processes that have shaped these adaptive molecules.

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Section: Resultsmentioning

confidence: 78%

Molecular Evolution of Lepidopteran Silk Proteins: Insights from the Ghost Moth, Hepialus californicus

et al. 2010

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“…In contrast, that of the mulberry silkworm, Bombyx mori ( B. mori ) SF, mainly consists of a (GAGAGS) n repeat sequence [6,7]. This characteristic assembly in the primary structure of S. c. ricini SF is almost similar to that of SF derived from silks produced by other Saturniidae wild silkworms such as Antheraea pernyi ( A. pernyi ) [8,9], Antheraea yamamai ( A. yamamai ) [10], Antheraea assama ( A. assama ) [11] and Antheraea mylitta ( A. mylitta ) [12], as well as the major ampullate (MA) silk of spiders (although their PA sequences are shorter, Ala (5-6) ) [13,14]. Similar to the PA sequences in S. c. ricini and other native wild SF, X-ray diffraction, and infrared, Raman and solid-state NMR spectroscopy studies [15,16,17,18,19,20,21,22,23,24] have shown the (GAGAGS) n repeat sequence regions in B. mori silk SF to primarily contribute to the formation of β -sheets [17,19,20,21,25,26].…”

Section: Introductionmentioning

confidence: 99%

Aggregation State of Residual α-Helices and Their Influence on Physical Properties of S. c. ricini Native Fiber

et al. 2019

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Formation of the α-helical conformation in the poly-l-alanine (PA) sequence regions, subsequent structural transition to β-sheet during natural spinning, and presence of residual α-helices in Samia cynthia ricini (S. c. ricini) native silk fiber have been experimentally proven. However, the aggregation state of the residual α-helices, and their influence on the mechanical deformation behavior in native fiber remain unclear. Here we show that the α-helices form an ordered aggregation state with a hexagonal packing in the aqueous solution, some of which remain during natural spinning. X-ray scattering and differential scanning calorimetry (DSC) analyses revealed occurrence of a structural transition of the residual α-helices to the β-sheet structure, accompanied by disappearance of the plateau region in the force-strain curve, due to heat-treatment at ~220 °C. On the basis of X-ray scattering before and after tensile stretching of S. c. ricini native silk, a direct connection between the plateau region and the α-helix to β-sheet structural transition was confirmed. Our findings demonstrate the importance of the PA sequence regions in fiber structure formation and their influence on the tensile deformation behavior of S. c. ricini silk, features believed to be essentially similar in other saturniid silks. We strongly believe the residual ordered α-helices to be strategically and systematically designed by S. c. ricini silkworms to impart flexibility in native silk fiber. We anticipate that these knowledge forms a basis for fruitful strategies in the design and development of amino acid sequences for artificial silks with desired mechanical properties.

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“…Bombyx mori silk fibroin has been extensively used for biomaterials because it is readily obtainable on large quantities ad displays good biocompatibility and biodegradability, resulting in practicable cell adhesion and cell spreading, high proliferative and anti-thrombosis activities, and potent ability to induce tissue repair [1,2,3,4,5,6,7]. Wild silkworm species such as Antheraea yamamai , Antheraea pernyi , Antheraea mylitta , Antheraea assama , and Philosamia ricini secrete another type of silk fibroin with arginine-glycine-aspartate (RGD) motif repeats in the protein chain [8,9,10,11,12], which is absent in mulberry ( B. mori ) silk fibroin [13].…”

Section: Introductionmentioning

confidence: 99%

“…The RGD tripeptide is considered a recognition sequence for promoting cell adhesion, and was originally found in fibronectin, laminin, vitronectin, fibrin, and collagen, where it binds specifically to the cell surface [14]. RGD tripeptides in A. yamamai and A. pernyi silk fibroins have up to 14 and 12 repeats, respectively [8,9], and these silk fibroins display even higher cell affinity and hold greater promise for biomaterial applications than B. mori silk fibroin. Only a few studies have reported that regenerated RGD tripeptide-containing silk fibroin materials from wild silkworm species are potentially useful biomaterials, with satisfactory cytocompatibility and the ability to promote tissue remodeling [15,16,17].…”

Section: Introductionmentioning

confidence: 99%

An RGD-Containing Peptide Derived from Wild Silkworm Silk Fibroin Promotes Cell Adhesion and Spreading

Zhao

Wang

et al. 2018

Polymers

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Arginine-Glycine-Aspartate (RGD) tripeptide can promote cell adhesion when present in the amino acid of proteins such as fibronectin. In order to demonstrate the bioactivity of an RGD-containing silk protein, a gene encoding the RGD motif-containing peptide GSGAGGRGDGGYGSGSS (–RGD–) derived from nonmulberry silk was designed and cloned, then multimerised and inserted into a commercial pGEX expression vector for recombinant expression of (–RGD–)n peptides. Herein, we focus on two glutathione-S-transferase (GST)-tagged fusion proteins, GST–(–RGD–)4 and GST–(–RGD–)8, which were expressed in Escherichia coli BL21, purified by GST affinity chromatography, and analyzed with sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and mass spectrometry (MS). Target peptides (–RGD–)4 and (–RGD–)8 (6.03 and 11.5 kDa) were cleaved from the GST-tag by thrombin digestion, as verified with MS and SDS-PAGE. Isoelectric point analysis confirmed that target peptides were expressed and released in accordance with the original design. Target peptides self-assembled into a mainly α-helical structure, as determined by circular dichroism spectroscopy. Furthermore, (–RGD–)4 and (–RGD–)8 modified mulberry silk fibroin films were more effective for rapid cell adhesion, spreading and proliferative activity of L929 cells than some chemically synthesized RGD peptides modified and mulberry silk lacking the RGD motif.

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Cited by 38 publications

References 11 publications

Molecular Evolution of Lepidopteran Silk Proteins: Insights from the Ghost Moth, Hepialus californicus

Molecular Evolution of Lepidopteran Silk Proteins: Insights from the Ghost Moth, Hepialus californicus

Aggregation State of Residual α-Helices and Their Influence on Physical Properties of S. c. ricini Native Fiber

An RGD-Containing Peptide Derived from Wild Silkworm Silk Fibroin Promotes Cell Adhesion and Spreading

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