The Self-Assembling Peptide P-4 Prevents Collagen Proteolysis in Dentin.

J Dent Res

1 Department of Pediatric Dentistry, Piracicaba Dental School, University of Campinas-UNICAMP, Campinas, SP, Piracicaba, São Paulo, Brazil.

Published: March 2019

The major goal in restorative dentistry is to develop a true regenerative approach that fully recovers hydroxyapatite crystals within the caries lesion. Recently, a rationally designed self-assembling peptide P-4 (Ace-QQRFEWEFEQQ-NH) has been developed to enhance remineralization on initial caries lesions, yet its applicability on dentin tissues remains unclear. Thus, the present study investigated the interaction of P-4 with the organic dentin components as well as the effect of P-4 on the proteolytic activity, mechanical properties of the bonding interface, and nanoleakage evaluation to artificial caries-affected dentin. Surface plasmon resonance and atomic force microscopy indicated that P-4 binds to collagen type I fibers, increasing their width from 214 ± 4 nm to 308 ± 5 nm ( P < 0.0001). P-4 also increased the resistance of collagen type I fibers against the proteolytic activity of collagenases. The immediate treatment of artificial caries-affected dentin with P-4 enhanced the microtensile bonding strength of the bonding interface ( P < 0.0001), reaching values close to sound dentin and decreasing the proteolytic activity at the hybrid layer; however, such effects decreased after 6 mo of water storage ( P < 0.05). In conclusion, P-4 interacts with collagen type I, increasing the resistance of collagen fibers to proteolysis, and improves stability of the hybrid layer formed by artificial caries-affected dentin.

Download full-text PDF

Source
http://dx.doi.org/10.1177/0022034518817351DOI Listing

Publication Analysis

Top Keywords

proteolytic activity
12
artificial caries-affected
12
caries-affected dentin
12
collagen type
12
self-assembling peptide
8
p-4
8
peptide p-4
8
bonding interface
8
type fibers
8
resistance collagen
8

Similar Publications

ClpXP is a two-component mitochondrial matrix protease. The caseinolytic mitochondrial matrix peptidase chaperone subunit X (ClpX) recognizes and translocates protein substrates into the degradation chamber of the caseinolytic protease P (ClpP) for proteolysis. ClpXP degrades damaged respiratory chain proteins and is necessary for cancer cell survival.

View Article and Find Full Text PDF

Ubiquitin-conjugating enzymes (E2s) are key for protein turnover and quality control via ubiquitination. Some E2s also physically interact with the proteasome, but it remains undetermined which E2s maintain proteostasis during aging. Here, we find that E2s have diverse roles in handling a model aggregation-prone protein (huntingtin-polyQ) in the Drosophila retina: while some E2s mediate aggregate assembly, UBE2D/effete (eff) and other E2s are required for huntingtin-polyQ degradation.

View Article and Find Full Text PDF

Biochemical features and biotechnological potential of a proteolytic extract from a psychrophilic Antarctic bacterium.

Braz J Microbiol

January 2025

Laboratorio de Biocatalizadores y sus Aplicaciones, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Iguá 4225, Montevideo, Uruguay.

Proteases are hydrolases that act on peptide bonds, releasing amino acids and/or oligopeptides, and are involved in essential functions in all organisms. They represent an important segment of the global enzyme market, with applications in the food, leather, detergent, and pharmaceutical industries. Depending on their industrial use, proteases should exhibit high activity under extreme conditions, such as low temperatures, e.

View Article and Find Full Text PDF

Caspase 3-specific cleavage of ubiquitin-specific peptidase 48 enhances drug-induced apoptosis in AML.

Cancer Biol Ther

December 2025

National & Local Joint Engineering Research Center of Biodiagnosis and Biotherapy, Department of Hematology, Precision Medical Institute, The Second Affiliated Hospital of Xi'an Jiaotong University, Xi'an, Shaanxi, China.

Dysfunction or dysregulation of deubiquitination is closely related to the initiation and development of multiple cancers. Targeted regulation of deubiquitination has been recognized as an important strategy in tumor therapy. However, the mechanism by which drugs regulate deubiquitinase is not clear.

View Article and Find Full Text PDF

Type 3 deiodinase activation mediated by the Shh/Gli1 axis promotes sepsis-induced metabolic dysregulation in skeletal muscles.

Burns Trauma

January 2025

Department of Critical Care Medicine, Nanjing Drum Tower Hospital, Affiliated Hospital of Medical School, Nanjing University, No. 321 Zhongshan Road, Gulou District, Nanjing, Jiangsu 210008, China.

Background: Non-thyroidal illness syndrome is commonly observed in critically ill patients, characterized by the inactivation of systemic thyroid hormones (TH), which aggravates metabolic dysfunction. Recent evidence indicates that enhanced TH inactivation is mediated by the reactivation of type 3 deiodinase (Dio3) at the tissue level, culminating in a perturbed local metabolic equilibrium. This study assessed whether targeted inhibition of Dio3 can maintain tissue metabolic homeostasis under septic conditions and explored the mechanism behind Dio3 reactivation.

View Article and Find Full Text PDF

Want 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!