Hyaluronan biopolymers release water upon pH-induced gelation
نویسندگان
چکیده
منابع مشابه
Light-activated ionic gelation of common biopolymers.
Biopolymers such as alginate and pectin are well known for their ability to undergo gelation upon addition of multivalent cations such as calcium (Ca(2+)). Here, we report a simple way to activate such ionic gelation by UV irradiation. Our approach involves combining an insoluble salt of the cation (e.g., calcium carbonate, CaCO(3)) with an aqueous solution of the polymer (e.g., alginate) along...
متن کاملpH-induced contrast in viscoelasticity imaging of biopolymers.
Understanding contrast mechanisms and identifying discriminating features is at the heart of diagnostic imaging development. This paper focuses on how pH influences the viscoelastic properties of biopolymers to better understand the effects of extracellular pH on breast tumour elasticity imaging. Extracellular pH is known to decrease as much as 1 pH unit in breast tumours, thus creating a dange...
متن کاملpH and cation-induced thermodynamic stability of human hyaluronan binding protein 1 regulates its hyaluronan affinity.
Hyaluronan-binding protein 1 (HABP1) is a trimeric protein with high negative charges distributed asymmetrically along the faces of the molecule. Recently, we have reported that HABP1 exhibits a high degree of structural flexibility, which can be perturbed by ions under in vitro conditions near physiological pH (Jha, B. K., Salunke, D. M., and Datta, K. (2003) J. Biol. Chem. 278, 27464-27472). ...
متن کاملEntropy gain due to water release upon ligand binding
Experimental thermodynamic data of the ligand-receptor association showed that the entropy changes upon binding are positive and large enough to be important driving forces of the binding process for a considerable number of ligand-receptor complexes [1]. The expected source behind such an entropy increase is the release of the water molecules from the binding pocket and from around the ligand ...
متن کاملRefolding dynamics of stretched biopolymers upon force quench.
Single-molecule force spectroscopy methods can be used to generate folding trajectories of biopolymers from arbitrary regions of the folding landscape. We illustrate the complexity of the folding kinetics and generic aspects of the collapse of RNA and proteins upon force quench by using simulations of an RNA hairpin and theory based on the de Gennes model for homopolymer collapse. The folding t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Physical Chemistry Chemical Physics
سال: 2020
ISSN: 1463-9076,1463-9084
DOI: 10.1039/d0cp00215a