Structural Study of Irregular Amino Acid Sequences in the Heavy Chain of Bombyx mori Silk Fibroin

2005 ◽  
Vol 6 (5) ◽  
pp. 2563-2569 ◽  
Author(s):  
Sung-Won Ha ◽  
Hanna S. Gracz ◽  
Alan E. Tonelli ◽  
Samuel M. Hudson
Keyword(s):  
Amino Acid ◽  
Bombyx Mori ◽  
Structural Study ◽  
Silk Fibroin ◽  
Heavy Chain ◽  
Amino Acid Sequences ◽  
Bombyx Mori Silk

X-ray structural study of noncrystalline regenerated Bombyx mori silk fibroin

2004 ◽  
Vol 34 (5) ◽  
pp. 259-265 ◽  
Author(s):  
Hiroyuki Saitoh ◽  
Ken-ichi Ohshima ◽  
Kozo Tsubouchi ◽  
Yoko Takasu ◽  
Hiromi Yamada
Keyword(s):  
Bombyx Mori ◽  
Structural Study ◽  
Silk Fibroin ◽  
X Ray ◽  
Bombyx Mori Silk

Poly-L-alanylglycyl-L-alanylglycyl-L-serylglycine: A synthetic model of Bombyx mori Silk Fibroin

1966 ◽  
Vol 19 (3) ◽  
pp. 489 ◽  
Author(s):  
FHC Stewart
Keyword(s):  
Amino Acid ◽  
Bombyx Mori ◽  
Silk Fibroin ◽  
Amino Acid Residues ◽  
Protecting Group ◽  
Synthetic Model ◽  
Bombyx Mori Silk ◽  
Nitrophenyl Ester

The sequential polypeptide [Ala-Gly-Ala-Gly-Ser-Gly]n has been prepared by polymerization of a hexapeptide p-nitrophenyl ester. This polymer contains the repeating sequence of amino acid residues present in the crystalline regions of Bombyx mori silk fibroin. The o-nitrophenylsulphenyl amino-protecting group was used extensively in the synthesis of the hexapeptide active monomer from which the polypeptide was obtained.

The Amino Acid Composition of Bombyx mori Silk Fibroin and of Tussah Silk Fibroin

1955 ◽  
Vol 77 (14) ◽  
pp. 3908-3913 ◽  
Author(s):  
W. A. Schroeder ◽  
Lois M. Kay ◽  
Barry Lewis ◽  
Nancy Munger
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Bombyx Mori ◽  
Acid Composition ◽  
Silk Fibroin ◽  
Bombyx Mori Silk ◽  
Tussah Silk Fibroin

scholarly journals Mass-spectrometric determination of the amino acid sequences in peptides isolated from protein silk fibroin of Bombyx mori

1969 ◽  
Vol 114 (4) ◽  
pp. 695-702 ◽  
Author(s):  
A J Geddes ◽  
G N Graham ◽  
H R Morris ◽  
F. Lucas ◽  
M. Barber ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bombyx Mori ◽  
Silk Fibroin ◽  
Protein Hydrolysate ◽  
Exchange Chromatography ◽  
Mass Spectrometric ◽  
Amino Acid Sequences ◽  
Peptide Component ◽  
First Time

Several peptides were isolated from the protein silk fibroin of Bombyx mori by means of ion-exchange chromatography of a chymotryptic digest. The sequences of three of the peptides, Gly-Ala-Gly-Tyr, Gly-Val-Gly-Tyr and Gly-Ala-Gly-Ala-Gly-Ala-Gly-Tyr, were known from previous chemical work, but the sequence of the fourth, Gly-Ala-Gly-Val-Gly-Ala-Gly-Tyr, was previously only partially known. The necessary volatility for mass-spectrometric examination of the peptides was achieved by permethylation of the N-acetyl-peptide methyl ester derivatives. From the mass spectra it was possible to confirm the known sequences and to establish that of the partially known one. In one instance it was possible to deduce from the same mass spectrum the sequence of a main peptide component and that of a small amount of contaminating peptide. These results demonstrate for the first time the use of mass spectrometry in the determination of the amino acid sequences in peptides from a protein hydrolysate.

scholarly journals Oxygen Permeability of Silk Fibroin Hydrogels and Their Use as Materials for Contact Lenses: A Purposeful Analysis

Gels ◽  
2021 ◽  
Vol 7 (2) ◽  
pp. 58
Author(s):  
Traian V. Chirila
Keyword(s):  
Tissue Engineering ◽  
Bombyx Mori ◽  
Silk Fibroin ◽  
Biomedical Applications ◽  
Oxygen Permeability ◽  
Contact Lenses ◽  
The Past ◽  
Fibrous Protein ◽  
Silk Moth ◽  
Bombyx Mori Silk

Fibroin is a fibrous protein that can be conveniently isolated from the silk cocoons produced by the larvae of Bombyx mori silk moth. In its form as a hydrogel, Bombyx mori silk fibroin (BMSF) has been employed in a variety of biomedical applications. When used as substrates for biomaterial-cells constructs in tissue engineering, the oxygen transport characteristics of the BMSF membranes have proved so far to be adequate. However, over the past three decades the BMSF hydrogels have been proposed episodically as materials for the manufacture of contact lenses, an application that depends on substantially elevated oxygen permeability. This review will show that the literature published on the oxygen permeability of BMSF is both limited and controversial. Additionally, there is no evidence that contact lenses made from BMSF have ever reached commercialization. The existing literature is discussed critically, leading to the conclusion that BMSF hydrogels are unsuitable as materials for contact lenses, while also attempting to explain the scarcity of data regarding the oxygen permeability of BMSF. To the author’s knowledge, this review covers all publications related to the topic.

Immobilization of glucose oxidase on nonwoven fabrics with bombyx mori silk fibroin gel

1992 ◽  
Vol 46 (1) ◽  
pp. 49-53 ◽  
Author(s):  
Tetsuo Asakura ◽  
Motohiro Kitaguchi ◽  
Makoto Demura ◽  
Harutoshi Sakai ◽  
Keiichi Komatsu
Keyword(s):  
Glucose Oxidase ◽  
Bombyx Mori ◽  
Silk Fibroin ◽  
Nonwoven Fabrics ◽  
Bombyx Mori Silk

Nucleation of hydroxyapatite crystals by self-assembled Bombyx mori silk fibroin

2013 ◽  
Vol 51 (9) ◽  
pp. 742-748 ◽  
Author(s):  
Mingying Yang ◽  
Wen He ◽  
Yajun Shuai ◽  
Sijia Min ◽  
Liangjun Zhu
Keyword(s):  
Bombyx Mori ◽  
Silk Fibroin ◽  
Bombyx Mori Silk ◽  
Self Assembled ◽  
Hydroxyapatite Crystals
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