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Raman study of poly(alanine-glycine)-based peptides containing tyrosine, valine, and serine as model for the semicrystalline domains of Bombyx mori silk fibroin

Authors

  • Paola Taddei,

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    1. Dipartimento di Biochimica “G. Moruzzi,” Sezione di Chimica e Propedeutica Biochimica, Centro di Studi sulla Spettroscopia Raman, Università di Bologna, Via Belmeloro 8/2, 40126 Bologna, Italy
    • Dipartimento di Biochimica “G. Moruzzi,” Sezione di Chimica e Propedeutica Biochimica, Centro di Studi sulla Spettroscopia Raman, Università di Bologna, Via Belmeloro 8/2, 40126 Bologna, Italy
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  • Tetsuo Asakura,

    1. Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184, Japan
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  • Juming Yao,

    1. Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184, Japan
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  • Patrizia Monti

    1. Dipartimento di Biochimica “G. Moruzzi,” Sezione di Chimica e Propedeutica Biochimica, Centro di Studi sulla Spettroscopia Raman, Università di Bologna, Via Belmeloro 8/2, 40126 Bologna, Italy
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Abstract

For a deeper insight into the structure of Bombyx mori silk fibroin, some model peptides containing tyrosine (Y), valine (V), and serine (S) in the basic (AG)n sequence were synthesized by the solid-phase method and analyzed by Raman spectroscopy in order to clarify their conformation and to evaluate the formation and/or disruption of the ordered structure typical of B. mori silk fibroin upon incorporation of Y, V, and S residues into the basic (AG)n sequence. The Raman results indicated that the silk I structure remains stable only when the Y residue is positioned near the chain terminus; otherwise, a silk I → silk II conformational transition occurs. The peptides AGVGAGYGAGVGAGYGAGVGAGYG(AG)3 and (AG)3YG(AG)2VGYG(AG)3YG(AG)3 treated with LiBr revealed a prevalent silk II conformation; moreover, the former contained a higher amount of random coil than the latter. This result was explained in relation to the different degrees of interruption of the (AG)n sequence. The Raman analysis of the AGSGAG-containing samples confirmed that the AGSGAG hexapeptide is a good model for the silk II crystalline domain. As the number of AGSGAG repeating units decreased, the random coil content increased. The study of the Y domain (I850/I830 intensity ratio) allowed us to hypothesize that in the packing characteristic of Silk I and Silk II conformations the Y residues experience different environments and hydrogen-bonding arrangements; the packing typical of silk I structure traps the tyrosyl side chains in environments more unfavorable to phenoxyl hydrogen-bonding interactions. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004

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