The amino acid composition of major ampullate gland silk (dragline) of Nephila clavipes (Araneae, Tetragnathidae)

Amino acid composition of major ampullate gland silk (dragline) produced by the mature, female golden orb-weaving spider, Nephila clavipes was determined. Several solvents were applied in order to solubilize the spider silk. Although several strong acids and bases were able to solubilize silk, the p...

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Bibliographic Details
Published in:The Journal of arachnology 1990-01, Vol.18 (3), p.297-306
Main Authors: Lombardi, S.J. (US Army Natick Research, Development, and Engineering Center, Natick, MA), Kaplan, D.L
Format: Article
Language:English
Subjects:
ACIDE AMINE
AMINO ACIDS
AMINOACIDOS
ANIMAL GLANDS
ARANEAE
Chemical composition
GLANDE ANIMALE
GLANDULAS ANIMALES
Hydrolysis
Nephila clavipes
Property composition
SEDA
SILK
SILK GLANDS
Silkworms
SOIE
Solubilization
Spiders
Tetragnathidae
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Summary:Amino acid composition of major ampullate gland silk (dragline) produced by the mature, female golden orb-weaving spider, Nephila clavipes was determined. Several solvents were applied in order to solubilize the spider silk. Although several strong acids and bases were able to solubilize silk, the protein was apparently degraded by this treatment, as demonstrated by protein gel electrophoresis. Only a mixture of hydrochloric/propionic acid (50:50, v:v, final concentration 3N HCL/25% propionic acid) solubilized the silk while retaining the molecular weight integrity of the crystalline polymer. The results show that the major ampullate gland secretion is characterized by a high degree of small side chain amino acids (Ala, Gly, and Ser) and polar residues (Gly and Arg), comprising almost 75% of the total amino acids present. Contrary to published findings (Work and Young 1987), the composition of major ampullate gland silk appears to be uniform within the species. The composition of the secretion is discussed in relation to the known and implied functions of the major ampullate gland as well as in relation to the mechanical properties of the silk produced by orb-web building spiders.
ISSN:0161-8202
1937-2396