Occlusal loading and cross-linking effects on dentin collagen degradation in physiological conditions

2016 ◽  
Vol 32 (2) ◽  
pp. 192-199 ◽  
Author(s):  
Gianluca Turco ◽  
Andrea Frassetto ◽  
Luca Fontanive ◽  
Annalisa Mazzoni ◽  
Milena Cadenaro ◽  
...  
2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Hiroko Nagaoka ◽  
Hideaki Nagaoka ◽  
Ricardo Walter ◽  
Lee W. Boushell ◽  
Patricia A. Miguez ◽  
...  

Application of biomodification techniques to dentin can improve its biochemical and biomechanical properties. Several collagen cross-linking agents have been reported to strengthen the mechanical properties of dentin. However, the characteristics of collagen that has undergone agent-induced biomodification are not well understood. The objective of this study was to analyze the effects of a natural cross-linking agent, genipin (GE), on dentin discoloration, collagen stability, and changes in amino acid composition and lysyl oxidase mediated natural collagen cross-links. Dentin collagen obtained from extracted bovine teeth was treated with three different concentrations of GE (0.01%, 0.1%, and 0.5%) for several treatment times (0–24 h). Changes in biochemical properties of NaB3H4-reduced collagen were characterized by amino acid and cross-link analyses. The treatment of dentin collagen with GE resulted in a concentration- and time-dependent pigmentation and stability against bacterial collagenase. The lysyl oxidase-mediated trivalent mature cross-link, pyridinoline, showed no difference among all groups while the major divalent immature cross-link, dehydro-dihydroxylysinonorleucine/its ketoamine in collagen treated with 0.5% GE for 24 h, significantly decreased compared to control (P< 0.05). The newly formed GE-induced cross-links most likely involve lysine and hydroxylysine residues of collagen in a concentration-dependent manner. Some of these cross-links appear to be reducible and stabilized with NaB3H4.


2017 ◽  
Vol 13 (6) ◽  
pp. 1152-1156 ◽  
Author(s):  
Siddhant Sethi ◽  
Minako Ooe ◽  
Takashi Sakamoto ◽  
Kenzo Fujimoto

Guanine, when replaced with inosine in the photo-responsive ODN containing 3-cyanovinylcarbazole nucleoside (CNVK), can accelerate photo-mediated cytosine deamination by many-folds under physiological conditions.


Gels ◽  
2021 ◽  
Vol 7 (3) ◽  
pp. 124
Author(s):  
Luca Vaghi ◽  
Mauro Monti ◽  
Marcello Marelli ◽  
Elisa Motto ◽  
Antonio Papagni ◽  
...  

Gelatin is a costless polypeptide material of natural origin, able to form hydrogels that are potentially useful in biomaterial scaffold design for drug delivery, cell cultures, and tissue engineering. However, gelatin hydrogels are unstable at physiological conditions, losing their features only after a few minutes at 37 °C. Accordingly, treatments to address this issue are of great interest. In the present work, we propose for the first time the use of bi- and trifunctional tetrazoles, most of them unknown to date, for photoinduced gelatin cross-linking towards the production of physiologically stable hydrogels. Indeed, after UV-B irradiation, aryl tetrazoles generate a nitrilimine intermediate that is reactive towards different functionalities, some of them constitutively present in the amino acid side chains of gelatin. The efficacy of the treatment strictly depends on the structure of the cross-linking agent used, and substantial improved stability was observed by switching from bifunctional to trifunctional cross-linkers.


2021 ◽  
Vol 17 (9) ◽  
pp. 1798-1805
Author(s):  
Damien Phakousonh ◽  
Yale Wang ◽  
Sabrina Schlicht ◽  
Sam Wiskirchen ◽  
Trevor Bos ◽  
...  

A pectin-oligochitosan microcapsule system has recently been developed for novel oxygen therapeutic design. To improve the stability of the pectin-oligochitosan microcapsules in physiological conditions, both covalent (glutaraldehyde) and noncovalent (Mn2+ and Ca2+) cross-linkers were tested. The chemistry and morphology of the microcapsules were studied using FTIR and SEM, respectively. Results showed that glutaraldehyde is an effective cross-linker, even at low concentrations and short incubation times, and the glutaraldehyde cross-linking does not negatively impact the morphology of the microcapsules. Moreover, it was confirmed that the hemoglobin could be retained within the microcapsules with a minimal release.


2017 ◽  
Vol 33 (10) ◽  
pp. 1103-1109 ◽  
Author(s):  
M.A. Moreira ◽  
N.O. Souza ◽  
R.S. Sousa ◽  
D.Q. Freitas ◽  
M.V. Lemos ◽  
...  

2013 ◽  
Vol 29 ◽  
pp. e93
Author(s):  
A. Frassetto ◽  
G. Turco ◽  
A. Mazzoni ◽  
M. Cadenaro ◽  
F.R. Tay ◽  
...  

1997 ◽  
Vol 8 (8) ◽  
pp. 1559-1573 ◽  
Author(s):  
D K Eggers ◽  
W J Welch ◽  
W J Hansen

Folding of newly synthesized proteins in vivo is believed to be facilitated by the cooperative interaction of a defined group of proteins known as molecular chaperones. We investigated the direct interaction of chaperones with nascent polypeptides in the cytosol of mammalian cells by multiple methods. A new approach using a polyclonal antibody to puromycin allowed us to tag and capture a population of truncated nascent polypeptides with no bias as to the identity of the bound chaperones. In addition, antibodies that recognize the cytosolic chaperones hsp70, CCT (TRiC), hsp40, p48 (Hip), and hsp90 were compared on the basis of their ability to coprecipitate nascent polypeptides, both before and after chemical cross-linking. By all three approaches, hsp70 was found to be the predominant chaperone bound to nascent polypeptides. The interaction between hsp70 and nascent polypeptides is apparently dynamic under physiological conditions but can be stabilized by depletion of ATP or by cross-linking. The cytosolic chaperonin CCT was found to bind primarily to full-length, newly synthesized actin, and tubulin. We demonstrate and caution that nascent polypeptides have a propensity for binding many proteins nonspecifically in cell lysates. Although current models of protein folding in vivo have described additional components in contact with nascent polypeptides, our data indicate that the hsp70 and, perhaps, the hsp90 families are the predominant classes of molecular chaperones that interact with the general population of cytosolic nascent polypeptides.


2012 ◽  
Vol 38 (9) ◽  
pp. 1227-1232 ◽  
Author(s):  
Raquel Osorio ◽  
Monica Yamauti ◽  
Salvatore Sauro ◽  
Thimoty F. Watson ◽  
Manuel Toledano

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