Abstract
preColD, a mussel byssus derived structural protein with a central collagen, was successfully produced recombinantly in the yeastPichia pastoris. It shows stable beta-sheet secondary structure (based on its silk-like terminal domains) and undergoes fibrillization as the natural preCols.
Highlights
Several marine species produce a variety of distinct materials for underwater attachment with mechanical properties ranging from those of cement[1] to silk[2] to so er and more elastic materials.[3]
PreColD was cloned with an a-secretion factor inducing translocation into the endoplasmic reticulum (ER) and subsequent secretion via the Golgi apparatus
A single band at the expected molecular weight could be detected by SDS-PAGE (ESI Fig. S2†), suggesting that the recombinant preColD was successfully translocated into the endoplasmic reticulum (ER), had its secretion factor cleaved as expected, but could not be secreted due to unknown reasons
Summary
Several marine species produce a variety of distinct materials for underwater attachment with mechanical properties ranging from those of cement[1] to silk[2] to so er and more elastic materials.[3]. A single band at the expected molecular weight could be detected by SDS-PAGE (ESI Fig. S2†), suggesting that the recombinant preColD was successfully translocated into the endoplasmic reticulum (ER), had its secretion factor cleaved as expected, but could not be secreted due to unknown reasons.
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