Intermolecular hydrogen bonded and self-assembled β-pleated sheet structures of β-sulfidocarbonyls
作者:Sahid Hussain、Gopal Das、Mihir K. Chaudhuri
DOI:10.1016/j.molstruc.2006.10.038
日期:2007.6
Abstract The three crystalstructures of β-sulfidocarbonyls 1, 2 and 3 synthesized from the reaction of acryl amide with cystiene, 1,2-dithiol and 1,3-dithiols, respectively, in water catalyzed by borax, have been determined at 273 K. The characteristic features of the structures are self-assembly through intermolecularhydrogenbonding leading to infinite chains of molecules in one direction, in addition
The invention provides peptides that bind Tissue Factor Pathway Inhibitor (TFPI), including TFPI-inhibitory peptides, and compositions thereof. The peptides may be used to inhibit a TFPI, enhance thrombin formation in a clotting factor-deficient subject, increase blood clot formation in a subject, treat a blood coagulation disorder in a subject, purify TFPI, an identify a TFPI-binding compound.
The present invention provides a method for reducing the level of acrylamide in a food product, comprising: (a) applying an acrylamide reduction agent in alkaline solution onto a food material before heat treating the food material; and (b) heat treating the food material to form the finished food product, wherein due to application of the thiol agent in alkaline solution, the finished food product comprises reduced level of acrylamide compared to a product which has not been treated with the acrylamide reduction agent in alkaline solution before heating. In addition, the present invention provides a food production produced by the method of the present invention.