Structural characterization of the major ampullate silk spidroin-2 protein produced by the spider Nephila clavipes

Made available in DSpace on 2018-11-26T16:56:30Z (GMT). No. of bitstreams: 0 Previous issue date: 2016-10-01 Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Gert Lubec Proteomics Laboratory at the University of Vienna Major ampullate spidroin-2 (MaSp2) is one of the most important spider silk protein, but up to now no information is available regarding the post-translational modifications (PTMs) of this protein. A gel-based mass spectrometry strategy using collision-induced dissociation (CID) and electron-transfer dissociation (ETD) fragmentation methods was used to sequence Nephila clavipes MaSp2 (including the N- and C-terminal non repetitive domains, and the great part of the central core), and to assign a series of post-translational modifications (PTMs) on to the MaSp2 sequence. Two forms of this protein were identified, with different levels of phosphorylation along their sequences. These findings provide a basis for understanding mechanoelastic properties and can support the future design of recombinant spider silk proteins for biotechnological applications. (C) 2016 Elsevier B.V. All rights reserved. Sao Paulo State Univ, Inst Biosci Rio Claro, Dept Biol, Ctr Study Social Insects, BR-13500 Rio Claro, SP, Brazil Univ Vienna, Dept Pharmaceut Chem, Althanstr 14, A-1090 Vienna, Austria Sao Paulo State Univ, Inst Biosci Rio Claro, Dept Biol, Ctr Study Social Insects, BR-13500 Rio Claro, SP, Brazil FAPESP: 2010/19051-6 FAPESP: 2011/51684-1 FAPESP: 2013/26451-9