FTIR Spectroscopic Characterization of Spider Silk of Family Lycosidae and Erasidae.
Keywords:
amide, amino acid, eresidae, lycosidae, silk, spiderAbstract
Spiders are unique in their ability to synthesize and utilize silk for various purposes. The primary structure of silk is its amino acid sequence, mainly consisting of highly repetitive blocks, which is why silks are often referred to as a block co-polymer. This attempt was made to characterize silk of Lycosiedae and Eresidae for the functional group amino acids by FTIR spectroscopy. The test results show that, the silk of Lycosideae contain strong –COOH asymmetrical vibration and –NH3 symmetrical bending vibration for Glutamic acid and Lysine, while in Eresidae, Arginine amino acid and with -NH2 medium bending vibrations. Both the silk samples show presence of Beta – sheet secondary protein structure. In Lycocedae, strong vibrations in Amide-I region, while in Eresidae, medium vibrations get observed. Amide-II band are absent in Eresidae. Amide –B band are observed in both the samples.
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References
Beard J (1992) Warding of bullets by a spider’s thread, New Scientist, 136,18.
Beek JD, Van S, Hess F, Vollrath and Meier BH (2002) The molecular Structure of spider dragline silk: Folding and orientation of the protein backbone. Proceeding of National Academy of Science (PNAS), USA. Current issue. Volume 99 (16) :10266-10271.
Cameron P Brown, Jennifer MacLeod, Heinz Amenitsch, Fernando Cacho Nerin , Harinderjit S Gill , Andrew J Price , Enrico Traversa, Silvia Licoccia and Federico Rosei. (2011) The critical role of water in spider silk and its consequence for protein mechanics. Nanoscale. Volume 3(9) :3805-11
Catherine LC, Christian Riekel, Marie E Herberstein Robert S Weber, David Kalpan and Naomi E. Pierce. (2000): Evidence of Diet Effects on the Composition of Silk Proteins Produced by Spiders. Mol Biol Evol. Volume 17 (12) :1904-1913.
Gosline JM, Gurette PA, Ortlepp CS, Savage KN (1990) The mechanical design of spider silk; from fibroin sequence to mechanical function. The Journal of Experimental Biolog. Volume 202 : 3295–3303.
Lombardi SJ and DL Kaplan. (1990) Amino acid composition of major ampullate gland silk (dragline) of Nephila clavipes (Araneae, Tetragnathidae). J. Arachnol. Volume 18 : 297-306
Normanteau J, Van Kessel C, Nicholson D, Rahasaar Routledge B, A. Fawcett, L. LiomCole, N. Salvain, T. Walker and , F. Borondies. (2014): Spider silk protein structure analysis by FTIR and STXM spectromicroscopy techniques. Canadian Young Scientist Journal, Bioscience.: 35-40.
Rengasamy, Raju Seenivasan, Manjeet Jassal and Chidambaram Rameshkumar (2005) Studies on structure and properties of nephila-spider Silk dragline, in AUTEX Research Journal, Volume 5 (1) : 30-39.
Saravanan D (2006) Spider Silk-Structure, properties and spinning. Journal of Textile Apparel, Technology and Management. Volume 5(1).
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