Collagen is the oldest and most abundant extracellular matrix protein that has found many applications in food, cosmetic, pharmaceutical, and biomedical industries First, an overview of the family of collagens and their respective structures, conformation, and biosynthesis is provided The advances and shortfalls of various collagen preparations (eg, mammalian/marine extracted collagen, cell-produced collagens, recombinant collagens, and collagen-like peptides) and crosslinking technologies (eg, chemical, physical, and biological) are then critically discussed Subsequently, an array of structural, thermal, mechanical, biochemical, and biological assays is examined, which are developed to analyze and characterize collagenous structures Lastly, a comprehensive review is provided on how advances in engineering, chemistry, and biology have enabled the development of bioactive, 3D structures (eg, tissue grafts, biomaterials, cell-assembled tissue equivalents) that closely imitate native supramolecular assemblies and have the capacity to deliver in a localized and sustained manner viable cell populations and/or bioactive/therapeutic molecules Clearly, collagens have a long history in both evolution and biotechnology and continue to offer both challenges and exciting opportunities in regenerative medicine as nature's biomaterial of choice

/pdf/the-collagen-suprafamily-from-biosynthesis-to-advanced-19x5x1lvm2.pdf

The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development

Tubulointerstitial disease, a prominent phenomenon in diabetic nephropathy, correlates with decline in renal function. The underlying pathogenic link between chronic hyperglycemia and the development of tubulointerstitial injury has not been fully elucidated, but myofibroblast formation represents a key step in the development of tubulointerstitial fibrosis. RAGE, the receptor for advanced glycation end products (AGEs), induces the expression of TGF-beta and other cytokines that are proposed to mediate the transdifferentiation of epithelial cells to form myofibroblasts. Here we report specific binding of (125)I-AGE-BSA to cell membranes prepared from a rat proximal tubule cell line and show that the binding site was RAGE. AGE exposure induced dose-dependent epithelial-myofibroblast transdifferentiation determined by morphological changes, de novo alpha smooth-muscle actin expression, and loss of epithelial E-cadherin staining. These effects could be blocked with neutralizing Ab's to RAGE or to TGF-beta. Transdifferentiation was also apparent in the proximal tubules of diabetic rats and in a renal biopsy from a patient with type 1 diabetes. The AGE cross-link breaker, phenyl-4,5-dimethylthiazolium bromide (ALT 711) reduced transdifferentiation in diabetic rats in association with reduced tubular AGE and TGF-beta expression. This study provides a novel mechanism to explain the development of tubulointerstitial disease in diabetic nephropathy and provides a new treatment target.

/pdf/advanced-glycation-end-products-cause-epithelial-1crh1vffo2.pdf

Advanced glycation end products cause epithelial-myofibroblast transdifferentiation via the receptor for advanced glycation end products (RAGE)

The Quantification of Protein Amino Groups by the Trinitrobenzenesulfonic Acid Method: A Reexamination

https://sites.ualberta.ca/~huludag/2009-2011/attachments/Xiong%20et%20al%202008.pdf

Biodegradable amphiphilic poly(ethylene oxide)-block-polyesters with grafted polyamines as supramolecular nanocarriers for efficient siRNA delivery

The functions of packaging materials are to prevent moisture loss, drip, reduce lipid oxidation, improve some of their sensorial properties (color, taste and smell) and provide microbial stability of foods. Edible films can be made from protein, polysaccharides and lipids or by combination of any of these to form a composite film. Nanocomposites are composite films made by incorporation of nanoparticles. Edible packaging and coating of the meat and meat products enhances the self-life by the incorporation of the active compound (such as antimicrobial and antioxidant compound) in to the packaging matrix. Incorporation of the some ingredients in the matrix may also improve the nutritional as well as sensory attributes of the packed products. Edible packaging material also reduces environmental pollution by overcoming the burden degradation as edible films are biodegradable and thus eco-friendly.

Comprehensive review on application of edible film on meat and meat products: An eco-friendly approach

This chapter describes the structures and main functional properties of the major whey proteins in order to try to establish relationships between protein structure and functionality. It discusses the effects of technological treatments on protein structure and their effects on functional properties and the behavior of whey protein ingredients in food products. Whey protein is a mixture of proteins with numerous and diverse functional properties and therefore may have many potential uses. The main proteins are β-lactoglobulin and a-lactalbumin. They represent approximately 70% of the total whey proteins and are responsible for the hydration, gelling, and surface-active properties of the whey protein ingredients. The structural properties of whey proteins depend on several environmental factors and also on technological treatments applied to milk. Thus, the impact of processing-induced structure modification on the functional properties should also be taken into account. In contrast, whey proteins adsorb and spread very slowly at the interface and create smaller foam particles.

Philippe Cayot

Papers

The Quantification of Protein Amino Groups by the Trinitrobenzenesulfonic Acid Method: A Reexamination

Structure-Function Relationships of Whey Proteins

Purification of αs-, β-and κ-caseins by batchwise ion-exchange separation