scholarly journals Strongly Adhesive and Antimicrobial Peptide-Loaded, Alginate–Catechol-Based Gels for Application against Periimplantitis

2021 ◽  
Vol 11 (21) ◽  
pp. 10050
Author(s):  
Sébastien Baixe ◽  
Vincent Ball ◽  
Loïc Jierry ◽  
Sarah Cianférani ◽  
Jean-Marc Strub ◽  
...  

Background: Periimplantitis is a disease linked to oral virulent bacteria such as P. gingivalis that grow in dental implants surrounding tissues and between implants and abutments. Antimicrobial gels previously described to fill these sites lose their effectiveness and resorb over time. Objective: Characterization of biophysical and antimicrobial properties of an original hydrogel, Alginate–Catechol (Alg–Cat), combined to D-Cateslytin (D-CTL). Methods: Gelation kinetics, frequency and strain sweep measurements were performed by rheology. Antibacterial activity of the gels was tested against P. gingivalis, and the MIC was determined. Peptides released from the gels were purified by HPLC and characterized by MALDI–TOF mass spectrometry. The behavior of bacteria in contact with the gel was observed using optical and electronic microscopy (SEM and TEM). Results: Gelation was fast and was achieved in 2 min with a storage modulus between 25 and 30 Pa. The gels were stable under strain and showed an adhesive potential reinforced with aging at 18 h (5.4 kPa) under a slow retraction speed (4 J·m−2 at 10 µm/s) with a mixed rupture profile (adhesive/cohesive). The MIC of D-CTL inside the Alg–Cat gel against P. gingivalis was equal to 470 µg·mL−1 after 24 h. Peptides recovered in the supernatant and inside the gel were fragmented, most of them conserving the ⍺-helix active site. No bacteria were visualized at the surface and inside the gel after 24 h. This gel is promising for clinical application for the prevention of periimplantitis.

2011 ◽  
Vol 6 (1) ◽  
pp. 111-120 ◽  
Author(s):  
Oliver Schilling ◽  
Pitter F Huesgen ◽  
Olivier Barré ◽  
Ulrich auf dem Keller ◽  
Christopher M Overall

2020 ◽  
Author(s):  
Tessa B. Moyer ◽  
Nicole C. Parsley ◽  
Patric W. Sadecki ◽  
Wyatt J. Schug ◽  
Leslie M. Hicks

Strategies to accelerate natural product peptide characterization.


2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Laura De Clerck ◽  
Jasin Taelman ◽  
Mina Popovic ◽  
Sander Willems ◽  
Margot Van der Jeught ◽  
...  

AbstractRecent progress has enabled the conversion of primed human embryonic stem cells (hESCs) to the naive state of pluripotency, resembling the well-characterized naive mouse ESCs (mESCs). However, a thorough histone epigenetic characterization of this conversion process is currently lacking, while its likeness to the mouse model has not been clearly established. Here, we profile the histone epigenome of hESCs during conversion in a time-resolved experimental design, using an untargeted mass spectrometry-based approach. In total, 23 histone post-translational modifications (hPTMs) changed significantly over time. H3K27Me3 was the most prominently increasing marker hPTM in naive hESCs. This is in line with previous reports in mouse, prompting us to compare all the shared hPTM fold changes between mouse and human, revealing a set of conserved hPTM markers for the naive state. Principally, we present the first roadmap of the changing human histone epigenome during the conversion of hESCs from the primed to the naive state. This further revealed similarities with mouse, which hint at a conserved mammalian epigenetic signature of the ground state of pluripotency.


2013 ◽  
Vol 5 (8) ◽  
pp. 1005-1010
Author(s):  
Lili Jin ◽  
Dezheng Yuan ◽  
Yu Wang ◽  
Chao Jiang ◽  
Zheng Wang ◽  
...  

RSC Advances ◽  
2015 ◽  
Vol 5 (93) ◽  
pp. 76107-76115 ◽  
Author(s):  
Hani Nasser Abdelhamid ◽  
Hui-Fen Wu

Synthesis and characterization of quantum dot modified mercaptopropionic acid (CdS@MPA) and its application in laser soft desorption/ionization for labile metal–drug interactions is reported.


1986 ◽  
Vol 56 (03) ◽  
pp. 349-352 ◽  
Author(s):  
A Tripodi ◽  
A Krachmalnicoff ◽  
P M Mannucci

SummaryFour members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and halfnormal antithrombin activity with or without heparin. Anti-factor Xa activities were consistently borderline low (about 70% of normal). For the propositus’ plasma and serum the patterns of antithrombin III in crossed-immunoelectrophoresis with or without heparin were indistinguishable from those of normal plasma or serum. A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography. Affinity adsorption of the propositus’ plasma to human α-thrombin immobilized on sepharose beads revealed defective binding of the anti thrombin III to thrombin-sepharose. Hence the molecular defect of this variant appears to be at the active site responsible for binding and neutralizing thrombin, thus accounting for the low thrombin inhibitory activity.


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