An investigation of the structure of silk fibroin

Marsh, Richard E.; Corey, Robert B.; Pauling, Linus

doi:10.1016/0006-3002(55)90178-5

Cited by 683 publications

(613 citation statements)

References 28 publications

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“…The highly organized crystalline regions were suggested to confer the toughness and the interspersed "amorphous" regions the elasticity of the silk fiber. The distance between ␤-sheets in the silk crystallites of Bombyx mori (family Bombycidae) corresponded to hydrogen bridges between side chains of glycine and alanine residues whereas in the silk of Antheraea pernyi (family Saturniidae) to interactions between alanine-alanine residues (2,3). These conclusions were consistent with the total amino acid composition of the respective silk.…”

supporting

confidence: 69%

“…2 To attest if the differences were due to repeat variation in different gene sections, we set out to examine cDNAs derived from the 3Ј end of the gene. The first strand cDNA was synthesized from total silk gland RNA with the aid of the F2 forward primer and the Trikant reverse primer.…”

Section: Resultsmentioning

confidence: 99%

“…In addition to the newly generated sequences, thorough analysis was applied to the E. kuehniella tags deposited in GenBank TM . 2 The conceptual translations of aligned tags revealed irregularities that could be traced to false frameshifts, obviously resulting from software interpretation of strong sequencer signals as nucleotide doublings. Some of these errors could be resolved and the continuity of the reading frames restored (Fig.…”

Section: Methodsmentioning

confidence: 99%

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Correlation between Fibroin Amino Acid Sequence and Physical Silk Properties

Fedic

Z̆urovec

Sehnal

2003

Journal of Biological Chemistry

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The fiber properties of lepidopteran silk depend on the amino acid repeats that interact during H-fibroin polymerization. The aim of our research was to relate repeat composition to insect biology and fiber strength. Representative regions of the H-fibroin genes were sequenced and analyzed in three pyralid species: wax moth (Galleria mellonella), European flour moth (Ephestia kuehniella), and Indian meal moth (Plodia interpunctella). The amino acid repeats are species-specific, evidently a diversification of an ancestral region of 43 residues, and include three types of regularly dispersed motifs: modifications of GSSAASAA sequence, stretches of tripeptides GXZ where X and Z represent bulky residues, and sequences similar to PVIVIEE. No concatenations of GX dipeptide or alanine, which are typical for Bombyx silkworms and Antheraea silk moths, respectively, were found. Despite different repeat structure, the silks of G. mellonella and E. kuehniella exhibit similar tensile strength as the Bombyx and Antheraea silks. We suggest that in these latter two species, variations in the repeat length obstruct repeat alignment, but sufficiently long stretches of iterated residues get superposed to interact. In the pyralid H-fibroins, interactions of the widely separated and diverse motifs depend on the precision of repeat matching; silk is strong in G. mellonella and E. kuehniella, with 2-3 types of long homogenous repeats, and nearly 10 times weaker in P. interpunctella, with seven types of shorter erratic repeats. The high proportion of large amino acids in the H-fibroin of pyralids has probably evolved in connection with the spinning habit of caterpillars that live in protective silk tubes and spin continuously, enlarging the tubes on one end and partly devouring the other one. The silk serves as a depot of energetically rich and essential amino acids that may be scarce in the diet.

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supporting

confidence: 69%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Correlation between Fibroin Amino Acid Sequence and Physical Silk Properties

Fedic

Z̆urovec

Sehnal

2003

Journal of Biological Chemistry

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“…As the major secondary structure is b-sheet, the spectra indicate that they are mainly oriented parallel to the fiber axis, in agreement with X-ray diffraction results. 27,28 A similar reasoning can be applied to the amide III band and leads to the same conclusion. Indeed, the amide III band has a strong contribution of the C-N stretching vibration, i.e., mainly along the polypeptide chain.…”

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confidence: 59%

Structure of silk by raman spectromicroscopy: From the spinning glands to the fibers

et al. 2011

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Raman spectroscopy has long been proved to be a useful tool to study the conformation of protein‐based materials such as silk. Thanks to recent developments, linearly polarized Raman spectromicroscopy has appeared very efficient to characterize the molecular structure of native single silk fibers and spinning dopes because it can provide information relative to the protein secondary structure, molecular orientation, and amino acid composition. This review will describe recent advances in the study of the structure of silk by Raman spectromicroscopy. A particular emphasis is put on the spider dragline and silkworm cocoon threads, other fibers spun by orb‐weaving spiders, the spinning dope contained in their silk glands and the effect of mechanical deformation. Taken together, the results of the literature show that Raman spectromicroscopy is particularly efficient to investigate all aspects of silk structure and production. The data provided can lead to a better understanding of the structure of the silk dope, transformations occurring during the spinning process, and structure and mechanical properties of native fibers. © 2011 Wiley Periodicals, Inc. Biopolymers 97: 322–336, 2012.

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“…The study of its structures, chemical, physical and mechanical properties have been extensively reviewed by various authors [1][2][3].…”

Section: Introductionmentioning

confidence: 99%

Surface Morphology and Properties of Bombyx mori Silk Fibroin Fiber Treated with I 2-KI Aqueous Solution

Khan

Gotoh

Morikawa

et al. 2009

Textile Research Journal

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.jp ABSTRACTThe surface morphology, thermal and mechanical properties of Bombyx mori silk fibroin (SF) fiber treated with a 1.23 N iodine-potassium iodide (I 2 -KI) aqueous solution were investigated using scanning electron microscopy (SEM), atomic force microscopy (AFM), differential scanning calorimetry (DSC), thermogravimetric (TG) analysis, and tensile measurements to clarify the effects of the iodine treatment. SEM and AFM analyses indicated that the SF fiber surface became rougher by the absorption of polyiodide ions. The mechanical properties of iodinated SF showed an increase in Young's modulus, and strain remained constant although ultimate tensile strength slightly decreased. The thermal stability of SF molecules was greatly enhanced by iodine treatment. Iodinated SF fibers should be an attractive candidate for biomedical applications such as for producing antimicrobial filters, iodine containing wound-healing anion exchange fibers, etc.

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An investigation of the structure of silk fibroin

Cited by 683 publications

References 28 publications

Correlation between Fibroin Amino Acid Sequence and Physical Silk Properties

Correlation between Fibroin Amino Acid Sequence and Physical Silk Properties

Structure of silk by raman spectromicroscopy: From the spinning glands to the fibers

Surface Morphology and Properties of Bombyx mori Silk Fibroin Fiber Treated with I 2-KI Aqueous Solution

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