37 research outputs found
The Production and Application of Hydrogels for Wound Management: A Review
Wound treatment has increased in importance in the wound care sector due to the pervasiveness of chronic wounds in the high-risk population including, but not limited to, geriatric population, immunocompromised and obese patients. Furthermore, the number of people diagnosed with diabetes is rapidly growing. According to the World Health Organization (WHO), the global diabetic occurrence has increased from 4.7 in 1980 to 8.5 in 2014. As diabetes becomes a common medical condition, it has also become one of the major causes of chronic wounds which require specialised care to address patients’ unique needs. Wound dressings play a vital role in the wound healing process as they protect the wound site from the external environment. They are also capable of interacting with the wound bed in order to facilitate and accelerate the healing process. Advanced dressings such as hydrogels are designed to maintain a moist environment at the site of application and due to high water content are ideal candidates for wound management. Hydrogels can be used for both exudating or dry necrotic wounds. Additionally, hydrogels also demonstrate other unique features such as softness, malleability and biocompatibility. Nowadays, advanced wound care products make up around 7.1 billion of the global market and their production is growing at an annual rate of 8.3 with the market projected to be worth 12.5 billion by 2022. The presented review focuses on novel hydrogel wound dressings, their main characteristics and their wound management applications. It also describes recent methodologies used for their production and the future potential developments
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EFFECT OF WATER ON THE STRUCTURE OF A MODEL POLYPEPTIDE
Vibrational spectroscopy in conjunction with X-ray and gravimetric methods has been used to study the structural stability of a hydrated polypeptide prepared in a genetically engineered strain of Escherichia coli. The sample adopts a β-sheet conformation in the solid state with a well-defined crystalline stem length and fold surfaces believed to be decorated with carboxylic acid groups. Ionization and subsequent hydration of these acid groups are found to have a major effect on the crystal packing and chain conformation. We have also established that the structural changes accompanying hydration of this model polypeptide occur in a stepwise fashion. First, because of their high accessibility, the carboxylic acid or carboxylate groups on the lamellar surfaces can readily interact with water molecules. In the second step, water penetrates into the regions between the hydrogen-bonded sheets; however, the resulting expansion in the intersheet distance can occur without altering the chain conformation. Lastly, when the water content is high, the hydrogen-bonded sheets are disrupted, leading to a change in chain conformation from ,&strands to helical or disordered chains
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Crystalline aggregates of the repetitive polypeptide {(AlaGly)(3)GluGly(GlyAla)(3)GluGly](10): Structure and dynamics probed by C-13 magic angle spinning nuclear magnetic resonance spectroscopy
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A pH dependent coil-to-sheet transition in a periodic artificial protein adsorbed at the air-water interface
External infrared reflectance spectroscopy allows in situ determination of the conformational state of a periodic artificial protein adsorbed at the air−water interface. The protein, which consists of 36 copies of an octapeptide sequence [(AG)_3EG] constituted from alanine (A), glycine (G), and glutamic acid (E), adopts a random coil conformation in aqueous solution over a broad range of pH (5 < pH < 14). In contrast, the adsorbed chain undergoes a transition from a disordered (coil-like) state to a β-sheet conformation as the pH of the subphase is reduced. The conformational transition is offset by ca. 4 pH units from the titration curve of the polymer in aqueous solution, suggesting that the ionization behavior of the polymer is substantially perturbed by interfacial effects. In situ determination of the conformation of the adsorbed chain allows observation of a coil-to-sheet transition that is not observed in bulk solution
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