scholarly journals Highly stretchable, compressible, adhesive hydrogels with double network

2021 ◽  
Vol 28 (11) ◽  
Author(s):  
Cuiping Guo ◽  
Zhiwen Zeng ◽  
Shan Yu ◽  
Xiaoyan Zhou ◽  
Qunfeng Liu ◽  
...  

AbstractIn this work, a double network bovine serum albumin-polyacrylamide (BSA-PAM) adhesive hydrogel was fabricated, in which combination of physical interactions including hydrogen bonds and chain entanglements, and chemical covalent photo-crosslinking. The BSA-PAM hydrogel exhibited excellent mechanical and adhesive properties. The composite hydrogel not only demonstrated excellent tensile properties (maximum force elongation 1552%~2037%), but also displayed extremely high fatigue resistance even when subjected to compress strains of up to 85%. More importantly, the BSA-PAM hydrogel showed excellent adhesiveness to various substrates (90 kPa~150 kPa for glass and 9.74 kPa~35.09 kPa for pigskin). This work provided a facile way of fabricating tough, stretchable and adhesive BSA-PAM hydrogels.

2017 ◽  
Vol 33 (2) ◽  
pp. 224-236 ◽  
Author(s):  
Bahar Demirdirek ◽  
Kathryn E Uhrich

Physically crosslinked hydrogels were developed via solvent casting methods using a temperature-sensitive polymer, poly( N-isopropylacrylamide- co-acrylic acid), and a therapeutic polymer, salicylate-based poly(anhydride-esters), to concurrently release salicylic acid and bovine serum albumin in a sustained manner. The physical interactions between the two polymer systems were confirmed using Fourier transform infrared spectroscopy. The crosslinked polymers were porous, thus able to encapsulate bovine serum albumin (23 wt%) and then released the protein in a sustained fashion over 96 h. Concurrently, the hydrogel releases salicylic acid in a sustained manner up to 120 h. Hydrogel systems were cytocompatible at relevant therapeutic concentrations. These hydrogel systems can be used for simultaneous delivery of salicylic acid and protein to achieve synergic effects.


2014 ◽  
Vol 664 ◽  
pp. 402-409
Author(s):  
Qing Ming Wang ◽  
Jia Liu ◽  
Tian Xing Zhang ◽  
Feng Zhu ◽  
Xin Hui Tang

We investigated the mutual interaction of daidzin with bovine serum albumin (BSA) by fluorescence spectroscopy. The results revealed that daidzin cause the fluorescence quenching of BSA through a static quenching procedure. The Stern-Volmer quenching constant (Ksv) were calculated at different temperature. The binding site (n), apparent binding constant (Ka) and corresponding thermodynamic parameters △Go, △Ho, △Sowere calculated and the van der Waals interaction, hydrogen bonds and hydrophobic interactions play an important role in stabilizing the complex. Besides, we also studied the effect of Cu2+, Ni2+, Mn2+and Co2+on the binding constants between daidzin and BSA, it is shows that the binding of BSA and daidzin is strengthened in the presence metal ions.


2002 ◽  
Vol 724 ◽  
Author(s):  
Thibaud Coradin ◽  
Aurélie Coupé ◽  
Jacques Livage

AbstractThe interaction of DNA, alginate, Lysozyme and Bovine Serum Albumin with diluted solutions of sodium silicate was studied using the molybdosilicate method. DNA and alginate showed very weak interactions with silica precursors whereas both proteins were able to form silica gels. Both electrostatic interactions and hydrogen bonds are suggested to arise between peptide chain and polysilicates, bringing new informations on the nature of inorganic and bio-organic species involved in the natural biosilicification processes.


Author(s):  
G. D. Gagne ◽  
M. F. Miller

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.


1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.


1974 ◽  
Vol 75 (1) ◽  
pp. 133-140 ◽  
Author(s):  
B. E. Senior

ABSTRACT A radioimmunoassay was developed to measure the levels of oestrone and oestradiol in 0.5–1.0 ml of domestic fowl peripheral plasma. The oestrogens were extracted with diethyl ether, chromatographed on columns of Sephadex LH-20 and assayed with an antiserum prepared against oestradiol-17β-succinyl-bovine serum albumin using a 17 h incubation at 4°C. The specificity, sensitivity, precision and accuracy of the assays were satisfactory. Oestrogen concentrations were determined in the plasma of birds in various reproductive states. In laying hens the ranges of oestrone and oestradiol were 12–190 pg/ml and 29–327 pg/ml respectively. Levels in immature birds, in adult cockerels and in an ovariectomized hen were barely detectable. The mean concentrations of oestrone and oestradiol in the plasma of four non-laying hens (55 pg/ml and 72 pg/ml respectively) and one partially ovariectomized hen (71 pg/ml and 134 pg/ml respectively) were well within the range for laying hens. It is evident that the large, yolk-filled follicles are not the only source of oestrogens in the chicken ovary.


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