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Technology and Health Care : Official... 2021The false positive rate of the PPI test for the diagnosis of typical symptoms of gastroesophageal reflux disease (GERD) is extremely high.
BACKGROUND
The false positive rate of the PPI test for the diagnosis of typical symptoms of gastroesophageal reflux disease (GERD) is extremely high.
OBJECTIVE
This study aims to investigate the effect of the pepsin test on GERD and laparoscopy-assisted anti-reflux surgery for GERD.
METHODS
A total of 30 GERD patients were enrolled into this study, and the pre-diagnosis of GERD was determined by symptom evaluation, impedance-pH examination, gastroscopy and pepsin test. All patients underwent surgery.
RESULTS
Among the 30 GERD patients, 18 patients were male and 12 were female, and their average age was 58.2 + 12.6 years old. The patients were treated with laparoscopic fundoplication and hiatus hernia repair after preoperative assessment. A total of 28 patients were followed up, one patient developed recurrent symptoms, and one patient developed postoperative dysphagia and received non-operative treatment. Furthermore, the symptom scores were significantly lower at postoperative pepsin detection when compared to the scores before the operation (pepsin: preoperative: 148.8 ± 82.6, postoperative: 30.7 ± 24.6; t= 4.848, P= 0.000).
CONCLUSIONS
Laparoscopic fundoplication and hiatus hernia repair may effectively control the symptoms of GERD. Furthermore, the detection of pepsin is non-invasive and easy to operate.
Topics: Aged; Female; Fundoplication; Gastroesophageal Reflux; Humans; Laparoscopy; Male; Middle Aged; Pepsin A; Treatment Outcome
PubMed: 32741794
DOI: 10.3233/THC-192090 -
Luminescence : the Journal of... Sep 2019In this paper, the interactions of pepsin with fluoroquinolones, including norfloxacin (NFX) or ofloxacin (OFX), were investigated using fluorescence spectroscopy. The...
In this paper, the interactions of pepsin with fluoroquinolones, including norfloxacin (NFX) or ofloxacin (OFX), were investigated using fluorescence spectroscopy. The effects of NFX or OFX on pepsin showed that the molecular conformation of pepsin and the microenvironment of tryptophan residues were changed under mimicked physiological conditions. Static quenching was suggested as a factor. Quenching constants and binding constants were determined and thermodynamic parameters were calculated at three temperatures (25°C, 31°C and 37°C). Molecular interaction distances (binding distance r) were obtained. Binding was enthalpy driven and the process was spontaneous. Synchronous fluorescence, three-dimensional fluorescence spectroscopy and molecular simulation were used for analysis. Interactions were further tested using molecular modelling. Quenching and binding constants of NFX with pepsin were the highest when testing NFX/OFX/fleroxacin/gatifloxacin with pepsin combinations. NFX was the strongest quencher, and affinity of NFX for pepsin was higher than that of OFX/fleroxacin/gatifloxacin.
Topics: Anti-Bacterial Agents; Fleroxacin; Fluorescence; Fluoroquinolones; Kinetics; Molecular Conformation; Molecular Docking Simulation; Norfloxacin; Pepsin A; Protein Binding; Spectrometry, Fluorescence
PubMed: 31074200
DOI: 10.1002/bio.3642 -
Spectrochimica Acta. Part A, Molecular... May 2022In this study, the interaction between gold nanoparticles (AuNPs) and proteins (including lysozyme, trypsin, pepsin, γ-globulin and hemoglobin) was investigated by...
In this study, the interaction between gold nanoparticles (AuNPs) and proteins (including lysozyme, trypsin, pepsin, γ-globulin and hemoglobin) was investigated by UV-visible absorption spectroscopy, fluorescence spectroscopy, circular dichroism (CD) spectroscopy and protein activity assay. AuNPs was synthesized using reduction of HAuCl with sodium citrate. The formation of AuNPs was confirmed from the characteristic surface plasmon resonance band at 521 nm and transmission electron microscopy revealed the average particle size was about 10 nm. The results reveal that AuNPs can interact with proteins to form a "protein corona (PC)", but the protein concentration required to form a relatively stable PC is not the same. The quenching mechanism of proteins by AuNPs is arisen from static quenching. The binding constants of AuNPs with proteins are in the range from 10 to 10 L mol, and the order is pepsin > γ-globulin > hemoglobin > trypsin > lysozyme at 298 K. Van der Waals forces and hydrogen bonds are the main forces for the lysozyme-AuNPs system. The interaction between trypsin/pepsin/γ-globulin/hemoglobin and AuNPs is mainly by hydrophobic interaction. The addition of AuNPs has an effect on the secondary structure of proteins as confirmed from CD spectra. The change in secondary structure of different proteins is different and seems to have little relation with the binding constant. The activity of lysozyme/trypsin/pepsin decreases with the addition of AuNPs.
Topics: Gold; Hemoglobins; Metal Nanoparticles; Muramidase; Pepsin A; Trypsin; gamma-Globulins
PubMed: 35149482
DOI: 10.1016/j.saa.2022.120983 -
Spectrochimica Acta. Part A, Molecular... Sep 2021Naringenin and naringin are two natural compounds with important health benefits, whether as food or drug. It is necessary to study the interactions between...
Naringenin and naringin are two natural compounds with important health benefits, whether as food or drug. It is necessary to study the interactions between naringenin/naringin and digestive proteases, such as trypsin and pepsin. In this study, the bindings of naringenin and naringin to trypsin and pepsin were investigated using multi-spectroscopy analysis and computational modeling approaches. Fluorescence experiments indicate that both naringenin and naringin can quench the intrinsic fluorescence of trypsin/pepsin via static quenching mechanism. Naringin binds trypsin/pepsin in a more firmly way than naringenin. Thermodynamic analysis reveals that the interactions of naringenin/naringin and trypsin/pepsin are synergistically driven by enthalpy and entropy, and the major driving forces are hydrophobic, electrostatic interactions and hydrogen bonding. Synchronous fluorescence spectroscopy, circular dichroism spectroscopy and FT-IR show that naringenin/naringin may induce microenvironmental and conformational changes of trypsin and pepsin. Molecular docking reveals that naringenin binds in the close vicinity of the active site (Ser-195) of trypsin and Asp-32 (the catalytic activity of pepsin) appears in naringin-pepsin system. The direct interactions between naringenin or naringin and catalytic amino acid residues will inhibit the catalytic activity of trypsin and pepsin, respectively. The results of molecular dynamic simulation validate the reliability of the docking results.
Topics: Circular Dichroism; Flavanones; Molecular Docking Simulation; Pepsin A; Protein Binding; Reproducibility of Results; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Trypsin
PubMed: 33957444
DOI: 10.1016/j.saa.2021.119859 -
Neurogastroenterology and Motility Sep 2023Peptest is a noninvasive and convenient diagnostic kit for gastroesophageal reflux disease (GERD). We aimed to explore the application value of Peptest in the diagnosis...
BACKGROUND
Peptest is a noninvasive and convenient diagnostic kit for gastroesophageal reflux disease (GERD). We aimed to explore the application value of Peptest in the diagnosis of GERD.
METHODS
Patients suspected of GERD all completed 24 h pH-impedance monitoring (24 h MII-pH) and then took proton pump inhibitor (PPI) 2 weeks. The postprandial, post-symptom and random salivary samples were taken. Receiver operating characteristic analysis was used to identify the best cutoff value of Peptest, to differentiate GERD patients from non-GERD patients and the optimal sampling time of Peptest was analyzed. Reflux characteristics and esophageal motility between Peptest (+) group and Peptest (-) group were compared in negative 24 h MII-pH patients. Peptest concentration were compared among non-reflux, distal reflux, and proximal reflux groups according to 24 h MII-pH curve.
RESULTS
The area under the curve of post-symptom Peptest was highest in three time points and the diagnostic specificity was 81.0% and sensitivity was 53.3% with the diagnostic value of 86 ng/mL. Compared with negative Peptest group, distal mean nocturnal baseline impedance was significantly lower, gastroesophageal junction contractile integral was substantially lower in positive Peptest group in negative 24 h MII-pH patients. The concentration of post-symptom and postprandial Peptest increased gradually in the non-reflux, distal reflux, and proximal reflux groups.
CONCLUSIONS & INFERENCES
Peptest has a relatively low diagnostic value for GERD. Post-symptom Peptset is the best sampling time with the optimal value of 86 ng/mL and may have auxiliary diagnostic value for negative 24 h MII-pH patients. Peptest may assist 24 h MII-pH in monitoring proximal reflux.
Topics: Humans; Pepsin A; Gastroesophageal Reflux; Esophagogastric Junction; Electric Impedance; Muscle Contraction; Esophageal pH Monitoring
PubMed: 37332241
DOI: 10.1111/nmo.14627 -
International Journal of Biological... Dec 2020Pepsin, as the main protease of the stomach, plays an important role in the digestion of food proteins into smaller peptides and performs about 20% of the digestive...
Pepsin, as the main protease of the stomach, plays an important role in the digestion of food proteins into smaller peptides and performs about 20% of the digestive function. The role of pepsin in the development of gastrointestinal ulcers has also been studied for many years. Edible drugs that enter the body through the gastrointestinal tract will interact with this enzyme as one of the first targets. Continuous and long-term usage of some drugs will cause chronic contact of the drug with this protein, and as a result, the structure and function of pepsin may be affected. Therefore, the possible effect of atenolol and diltiazem on the structure and activity of pepsin was studied. The interaction of drugs with pepsin was evaluated using various experimental methods including UV-Visible spectroscopy, fluorescence spectroscopy, FTIR and enzymatic activity along with computational approaches. It was showed that after binding of atenolol and diltiazem to pepsin, the inherent fluorescence of the protein is quenched. Determination of the thermodynamic parameters of interactions between atenolol and diltiazem with pepsin indicates that the major forces in the formation of the protein-drug complexes are hydrophobic forces and also atenolol has a stronger protein bonding than diltiazem. Additional tests also show that the protease activity of pepsin, decreases and increases in the presence of atenolol and diltiazem, respectively. Investigation of the FTIR spectrum of the protein in the presence and absence of atenolol and diltiazem show that in the presence of atenolol the structure of protein has slightly changed. Molecular modeling studies, in agreement with the experimental results, confirm the binding of atenolol and diltiazem to the enzyme pepsin and show that the drugs are bind close to the active site of the enzyme. Finally, from experimental and computational results, it can be concluded that atenolol and diltiazem interact with the pepsin and change its structure and protease activity.
Topics: Atenolol; Binding Sites; Catalytic Domain; Diltiazem; Humans; Hydrogen Bonding; Molecular Docking Simulation; Pepsin A; Peptide Hydrolases; Protein Binding; Spectrometry, Fluorescence; Structure-Activity Relationship
PubMed: 33096169
DOI: 10.1016/j.ijbiomac.2020.10.118 -
Otology & Neurotology : Official... Aug 2021To investigate the relationship between laryngopharyngeal reflux (LPR) and recurrent (ROM) or chronic otitis media with effusion (COME).
OBJECTIVES
To investigate the relationship between laryngopharyngeal reflux (LPR) and recurrent (ROM) or chronic otitis media with effusion (COME).
DATABASES
PubMed, Scopus, and Cochrane Library.
METHODS
Three authors searched articles published between January 1980 and September 2020 about the association between LPR and the development of recurrent or chronic otitis media. Inclusion, exclusion, diagnostic criteria, and clinical outcome evaluation of included studies were analyzed using PRISMA criteria. The bias analysis of included studies was evaluated with the Tool to assess Risk of Bias of the CLARITY group.
RESULTS
Twenty-six clinical and three experimental articles met our inclusion criteria, accounting for 1,624 children and 144 adults with COME or ROM. According to the pH study type, the prevalence of LPR and gastroesophageal reflux disease (GERD) in OM patients were 28.7% (range, 8-100%) and 40.7 (range, 18-64%), respectively. The majority of studies identified pepsin or pepsinogen in middle ear effusion, with a range of mean concentrations depending on the technique used to measure pepsin. There was an important heterogeneity between studies regarding definition of COME, ROM, and LPR, exclusion criteria, methods used to measure pepsin/pepsinogen in middle ear secretions and outcome assessments.
CONCLUSION
The association between LPR and OM is still unclear. Future clinical and experimental studies are needed to investigate the association between LPR and OM in both children and adults through extensive gastric content analysis in middle ear suppurations and impedance-pH monitoring considering acid, weakly acid, and alkaline reflux events.
Topics: Child; Humans; Laryngopharyngeal Reflux; Otitis Media; Otitis Media with Effusion; Pepsin A; Pepsinogen A
PubMed: 33710157
DOI: 10.1097/MAO.0000000000003123 -
Scientific Reports Sep 2022Antimicrobial peptides (AMPs) are being developed as potent alternative treatments to conventional antibiotics which are unlikely to induce bacterial resistance. They...
Antimicrobial peptides (AMPs) are being developed as potent alternative treatments to conventional antibiotics which are unlikely to induce bacterial resistance. They can be designed and modified to possess several druggable properties. We report herein a novel hybrid peptide of modified aurein (A3) and cathelicidin (P7), or A3P7, by a flipping technique. It exhibited potent antibacterial activity against both Gram-negative and -positive pathogenic bacteria but had moderate hemolytic activity. To reduce the sequence length and toxicity, C-terminal truncation was serially performed and eight truncated derivatives (AP12-AP19) were obtained. They had significantly less hemolytic activity while preserving antibacterial activity. Secondary structures of the candidate peptides in environments simulating bacterial membranes (30 mM SDS and 50% TFE), determined by CD spectroscopy, showed α-helical structures consistent with predicted in silico 3D structural models. Among the peptides, AP19 demonstrated the best combination of broad-spectrum antibacterial activity (including toward Acinetobacter baumannii) and minimal hemolytic and cytotoxic activities. A D-form peptide (D-AP19), in which all L-enantiomers were substituted with the D-enantiomers, maintained antibacterial activity in the presence of pepsin, trypsin, proteinase K and human plasma. Both isomers exhibited potent antibacterial activity against multi-drug (MDR) and extensively-drug resistant (XDR) clinical isolates of A. baumannii comparable to the traditional antibiotic, meropenem. D-AP19 displayed rapid killing via membrane disruption and leakage of intracellular contents. Additionally, it showed a low tendency to induce bacterial resistance. Our work suggested that D-AP19 could be further optimized and developed as a novel compound potentially for fighting against MDR or XDR A. baumannii.
Topics: Humans; Acinetobacter baumannii; Anti-Bacterial Agents; Bacteria; Drug Resistance, Multiple, Bacterial; Endopeptidase K; Meropenem; Microbial Sensitivity Tests; Pepsin A; Peptide Hydrolases; Trypsin
PubMed: 36151303
DOI: 10.1038/s41598-022-20236-1 -
The Laryngoscope Apr 2020Laryngopharyngeal reflux (LPR) is a common upper airway disease. Salivary pepsin is a proposed marker for LPR; however, the optimal time for collection of specimens for...
OBJECTIVES
Laryngopharyngeal reflux (LPR) is a common upper airway disease. Salivary pepsin is a proposed marker for LPR; however, the optimal time for collection of specimens for pepsin detection and pepsin's presence in the oral and nasal secretions relative to concurrent multichannel intraluminal impedance-pH (MII-pH) monitoring are unknown.
STUDY DESIGN
Prospective case-control study with an experimental design.
METHODS
Patients undergoing MII-pH testing for evaluation of LPR and asymptomatic control subjects were selected. Nasal lavage and saliva samples were collected in the clinic prior to MII-pH probe placement. Additional saliva samples were obtained an hour after each meal and upon waking the following morning. Nasal lavage and salivary pepsin were measured by ELISA.
RESULTS
Twenty-six patients undergoing MII-pH testing and 13 reflux-free control patients were enrolled. Salivary pepsin was detected in 11 of 26 patients with suspected LPR and 0 of 13 controls. Pepsin was most frequently detected in the specimen provided upon waking at an average concentration of 186.9 ng/mL. A significant correlation was observed between salivary pepsin in waking samples to MII-pH measurements, including reflux bolus duration, and proximal and distal recumbent reflux episodes (P < 0.05). A significant correlation was also observed between salivary pepsin upon waking or sinus lavage and reflux symptom index (P < 0.05).
CONCLUSION
Pepsin in salivary and nasal lavage samples demonstrated an association with MII-pH-documented LPR. Pepsin detection was most frequent in morning samples, supporting use of morning salivary pepsin levels as a potential noninvasive technique for LPR diagnosis.
LEVEL OF EVIDENCE
2 Laryngoscope, 130:961-966, 2020.
Topics: Adult; Biomarkers; Case-Control Studies; Electric Impedance; Enzyme-Linked Immunosorbent Assay; Esophageal pH Monitoring; Esophagus; Female; Follow-Up Studies; Humans; Hydrogen-Ion Concentration; Laryngopharyngeal Reflux; Male; Middle Aged; Nasal Lavage; Nasal Mucosa; Pepsin A; Prospective Studies; Saliva
PubMed: 31329290
DOI: 10.1002/lary.28182 -
Biomacromolecules Dec 2023Solubilized, gel-forming decellularized extracellular matrix (dECM) is used in a wide range of basic and translational research and due to its inherent bioactivity can...
Solubilized, gel-forming decellularized extracellular matrix (dECM) is used in a wide range of basic and translational research and due to its inherent bioactivity can promote structural and functional tissue remodeling. The animal-derived protease pepsin has become the standard proteolytic enzyme for the solubilization of almost all types of collagen-based dECM. In this study, pepsin was compared with papain, α-amylase, and collagenase for their potential to solubilize porcine liver dECM. Maximum preservation of bioactive components and native dECM properties was used as a decisive criterion for further application of the enzymes, with emphasis on minimal destruction of the protein structure and maintained capacity for physical thermogelation at neutral pH. The solubilized dECM digests, and/or their physically gelled hydrogels were characterized for their rheological properties, gelation kinetics, GAG content, proteomic composition, and growth factor profile. This study highlights papain as a plant-derived enzyme that can serve as a cost-effective alternative to animal-derived pepsin for the efficient solubilization of dECM. The resulting homogeneous papain-digested dECM preserved its thermally triggered gelation properties similar to pepsin digests, and the corresponding dECM hydrogels demonstrated their enhanced bioadhesiveness in single-cell force spectroscopy experiments with fibroblasts. The viability and proliferation of human HepaRG cells on dECM gels were similar to those on pure rat tail collagen type I gels. Papain is not only highly effective and economically attractive for dECM solubilization but also particularly interesting when digesting human-tissue-derived dECM for regenerative applications, where animal-derived materials are to be avoided.
Topics: Rats; Swine; Humans; Animals; Extracellular Matrix; Papain; Decellularized Extracellular Matrix; Pepsin A; Proteomics; Hydrogels; Tissue Engineering; Tissue Scaffolds
PubMed: 38009757
DOI: 10.1021/acs.biomac.3c00602