By the same authors

From the same journal

Proteomic Profiling of the Photo-oxidation of Silk Fibroin: Implications for Historic Tin-Weighted Silk

Research output: Contribution to journalArticle

Author(s)

Department/unit(s)

Publication details

JournalJOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
DateIn preparation - Sep 2012
Issue number5
Volume88
Number of pages10
Pages (from-to)1217-1226
Original languageEnglish

Abstract

The stability of silk proteins to ultraviolet light is an issue of significant concern in both the appearance retention of silk-derived products and the preservation of historic silk textiles. Until now, evaluation of silk degradation has only been performed at the holistic, rather than molecular level. This paper describes the first proteomic profiling of silk photo-oxidation, characterising protein primary level modification leading to coloration changes, and evaluating the effects of tin weighting on photodegradation. Heavy chain fibroin, the main proteinaceous component of the silk thread, is a repetitive, highly crystalline protein with a content rich in tyrosine. Photoproducts of tyrosine were characterised and the levels of oxidative modification at the protein primary structural level correlated with changes in coloration and tensile strength. The effect of tin as a weighting agent used on historical fabrics was examined. Tin-weighted fabrics were evaluated following two treatments (pink and dynamite) and proteomic analysis revealed a significant increase in oxidatively modified amino acid residues within the pink treated silk. These findings offer significant new insight into the molecular-level oxidation of silk proteins under UV exposure, and the effects of silk treatments in either exacerbating or ameliorating this degradation.

    Research areas

  • Silk fibroin, photoyellowing, photo-oxidation, tin weighting, historic textiles

Discover related content

Find related publications, people, projects, datasets and more using interactive charts.

View graph of relations