AI Article Synopsis
Article Abstract
In this study, we suggest a new biocomposite scaffold composed of gelatin/α-TCP (tricalcium phosphate)/SF (silk-fibroin) (GTS) which has enhanced mechanical strength and high level of cellular activity. To fabricate GTS scaffold, a temperature-controlled 3D printing process was used and appropriate printing conditions were selected based on rheological data. To show the feasibility as a biomedical scaffold for bone tissue regeneration, the various physical and biological results, using MG63 (osteoblast-like cells), of the GTS scaffold were compared with those of a pure gelatin (G) and gelatin/α-TCP (GT) composite scaffold. GTS scaffolds showed enhanced mechanical properties in dry and wet state compared to those of the G and GT scaffolds. Also, significantly high cell-proliferation and differentiation of MG63 cells were observed in the GTS scaffold. Therefore, the GTS composite scaffold will be one of highly potential biomaterials to be used in bone regeneration.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.ijbiomac.2017.09.030 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
New Pyridyl and Dihydroisoquinoline Alkaloids Isolated from the Chevron Nemertean .
Mar Drugs
March 2024
Mass Spectrometry Research and Education Center, Department of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Nemertean worms contain toxins that are used to paralyze their prey and to deter potential predators. Hoplonemerteans often contain pyridyl alkaloids like anabaseine that act through nicotinic acetylcholine receptors and crustacean chemoreceptors. The chemical reactivity of anabaseine, the first nemertean alkaloid to be identified, has been exploited to make drug candidates selective for alpha7 subtype nAChRs.
View Article and Find Full Text PDFEngineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology.
Microb Cell Fact
March 2024
Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, 4301 West Markham St. / Biomed I, Room 511 / Little Rock, Little Rock, AR, 72205, USA.
Background: Bacterial surface glycans are assembled by glycosyltransferases (GTs) that transfer sugar monomers to long-chained lipid carriers. Most bacteria employ the 55-carbon chain undecaprenyl phosphate (Und-P) to scaffold glycan assembly. The amount of Und-P available for glycan synthesis is thought to be limited by the rate of Und-P synthesis and by competition for Und-P between phosphoglycosyl transferases (PGTs) and GTs that prime glycan assembly (which we collectively refer to as PGT/GTs).
View Article and Find Full Text PDFGlycosyltransferase 8 domain-containing protein 1 (GLT8D1) is a UDP-dependent galactosyltransferase.
Sci Rep
December 2023
Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, 2780-157, Oeiras, Portugal.
Glycosyltransferases (GTs) are enzymes that catalyze the formation of glycosidic bonds and hundreds of GTs have been identified so far in humans. Glycosyltransferase 8 domain-containing protein 1 (GLT8D1) has been associated with central nervous system diseases and cancer. However, evidence on its enzymatic properties, including its substrates, has been scarcely described.
View Article and Find Full Text PDFA "biphasic glycosyltransferase high-throughput screen" identifies novel anthraquinone glycosides in the diversification of phenolic natural products.
J Biol Chem
March 2023
Department of Biology, Centre for Applied Synthetic Biology, and Centre for Structural and Functional Genomics, Concordia University, Montreal, Quebec, Canada; Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec, Canada; PROTEO, Quebec Network for Research on Protein Function, Quebec City, Quebec, Canada. Electronic address:
The sugar moieties of many glycosylated small molecule natural products are essential for their biological activity. Glycosyltransferases (GTs) are enzymes responsible for installing these sugar moieties on a variety of biomolecules. Many GTs active on natural products are inherently substrate promiscuous and thus serve as useful tools in manipulating natural product glycosylation to generate new combinations of sugar units (glycones) and scaffold molecules (aglycones) in a process called glycodiversification.
View Article and Find Full Text PDFPromiscuity Characteristics of Versatile Plant Glycosyltransferases for Natural Product Glycodiversification.
ACS Synth Biol
February 2022
State Key Laboratory of Microbial Technology, Institute of Microbial Technology, Shandong University, 266237 Qingdao, P. R. China.
Glycodiversification can optimize the properties of pharmaceutical compounds, and versatile glycosyltransferases (GTs) are the key enzymatic toolkits to achieve this goal. Plant GTs in the GT1 family (GT1-pGTs) have attracted much attention due to their promising substrate promiscuity, but previous investigations on GT1-pGTs were mainly conducted sporadically and without systematic phylogenetic comparisons. In this study, we exemplified the phylogeny-guided characterization of highly promiscuous GT1-pGTs from the contemporary surge of genomic information.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!