Modification of bacterial cellulose using silk fibroin β-sheet crystals induced by ultrasonication

Silk fibroin (SF) has been continuously explored as a biomaterial due to its biocompatibility, tunability, and self-healing properties. In this work, we present a novel approach to the modification of bacterial cellulose (BC) with SF β-sheet dominant structures induced via ultrasonication. Secondary structure analysis through infrared spectroscopy, thioflavin T assay, and circular dichroism spectropolarimetry revealed a conversion of silk I to silk II structures within the protein mixture. Cold field emission scanning electron microscope images revealed the tightly packed fibers coated with the protein. Thermogravimetric curves demonstrated higher resistance to temperature degradation supplemented by broader and flatter DSC curves attributed to the highly bonded and dense composite. Successful conversion of amide I to amide II and amide III allowed for the more stable β-crystals to contribute to a more thermodynamically stable double-network hydrogel. The conversion of silk I to silk II structures offers a viable and highly biocompatible material that is both thermodynamically and biochemically stable for various potential biomedical applications

A History of Molecular Chaperone Structures in the Protein Data Bank

Thirty years ago a class of proteins was found to prevent the aggregation of Rubisco. These proteins’ ability to prevent unwanted associations led to their being called chaperones. These chaperone proteins also increased in expression as a response to heat shock, hence their label as heat shock proteins (Hsps). However, neither label encompasses the breadth of these proteins’ functional capabilities. The term “unfoldases” has been proposed, as this basic function is shared by most members of this protein family. Onto this is added specializations that allow the different family members to perform various cellular functions. This current article focuses on the resolved structural bases for these functions. It reviews the currently available molecular structures in the Protein Data Bank for several classes of Hsps (Hsp60, Hsp70, Hsp90, and Hsp104). When possible, it discusses the complete structures for these proteins, and the types of molecular machines to which they have been assigned. The structures of domains and the associated functions are discussed in order to illustrate the rationale for the proposed unfoldase function