Enzyme Responsive Vaginal Microbicide Gels Containing Maraviroc and Tenofovir Microspheres Designed for Acid Phosphatase-Triggered Release for Pre-Exposure Prophylaxis of HIV-1: A Comparative Analysis of a Bigel and Thermosensitive Gel

Gels ◽  
2021 ◽  
Vol 8 (1) ◽  
pp. 15
Author(s):  
Sabdat Ozichu Ekama ◽  
Margaret O. Ilomuanya ◽  
Chukwuemeka Paul Azubuike ◽  
James Babatunde Ayorinde ◽  
Oliver Chukwujekwu Ezechi ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Transport Mechanism ◽  
Seminal Fluid ◽  
Release Kinetics ◽  
Triggered Release ◽  
Thermosensitive Gel ◽  
Hela Cell Lines ◽  
Hiv 1 ◽  
Phosphatase Enzyme ◽  
Microbicide Gels

The challenges encountered with conventional microbicide gels has necessitated the quest for alternative options. This study aimed to formulate and evaluate a bigel and thermosensitive gel, designed to combat the challenges of leakage and short-residence time in the vagina. Ionic-gelation technique was used to formulate maraviroc and tenofovir microspheres. The microspheres were incorporated into a thermosensitive gel and bigel, then evaluated. Enzyme degradation assay was used to assess the effect of the acid phosphatase enzyme on the release profile of maraviroc and tenofovir microspheres. HIV efficacy and cytotoxicity of the microspheres were assessed using HIV-1-BaL virus strain and HeLa cell lines, respectively. Maraviroc and tenofovir release kinetics followed zero-order and Higuchi model kinetics. However, under the influence of the enzyme, maraviroc release was governed by first-order model, while tenofovir followed a super case II transport-mechanism. The altered mode of release and drug transport mechanism suggests a triggered release. The assay of the microspheres suspension on the HeLa cells did not show signs of cytotoxicity. The thermosensitive gel and bigel elicited a progressive decline in HIV infectivity, until at concentrations of 1 μg/mL and 0.1 μg/mL, respectively. The candidate vaginal gels have the potential for a triggered release by the acid phosphatase enzyme present in the seminal fluid, thus, serving as a strategic point to prevent HIV transmission.

Smartphone Based Highly Sensitive Visualized Detection of Acid Phosphatase Enzyme Activity

2021 ◽  
Author(s):  
Rui Li ◽  
Yanan Sun ◽  
Lihua Jin ◽  
Xiaohong Qiao ◽  
Cong Li ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Point Of Care ◽  
Rapid Development ◽  
Practical Application ◽  
Fast Analysis ◽  
Highly Sensitive ◽  
Visualized Detection ◽  
Sensitive Method ◽  
Phosphatase Enzyme

With the rapid development of point-of-care (POC) technologies, the improvement of sensitive method featured with fast analysis and affordable devices has become an emerging requirement for the practical application. In...

Detection of prostatic tissue and seminal plasma peptides reacting with human seminal fluid acid phosphatase antibodies

1986 ◽  
Vol 18 (11) ◽  
pp. 1005-1013 ◽  
Author(s):  
Radosława Kuciel ◽  
Izydor Apostoł ◽  
Ewa Wasylewska ◽  
Włodzimierz S. Ostrowski ◽  
Iga Steuden ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Seminal Plasma ◽  
Seminal Fluid ◽  
Prostatic Tissue

Physiological studies on trematodes: phosphatase systems in Gastrothylax crumenifer

Parasitology ◽  
1966 ◽  
Vol 56 (1) ◽  
pp. 105-110 ◽  
Author(s):  
Madan M. Goil
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Maximum Activity ◽  
Fluoride Ions ◽  
Gastrothylax Crumenifer ◽  
Biochemical Studies ◽  
Physiological Studies ◽  
Phosphatase Enzyme

Biochemical studies on the phosphatase systems of Gastrothylax crumenifer have been made. The maximum activity of the phosphatase enzyme was found to be at 5 pH. The action of magnesium and fluoride ions on the acid phosphatase activity shows that both act as inhibitors. The day-to-day variation in the phosphatase activity of the samples, as measured by block differences, was found to be significant at different pH levels. The heat denatured extract showed low and fairly constant acid phosphatase activity.

Development of a stable reference material for prostatic acid phosphatase.

1984 ◽  
Vol 30 (8) ◽  
pp. 1327-1331 ◽  
Author(s):  
P H Duncan ◽  
R L Van Etten ◽  
M L MacNeil ◽  
L M Shaw
Keyword(s):  
Catalytic Activity ◽  
Acid Phosphatase ◽  
Reference Material ◽  
Sodium Acetate ◽  
Seminal Fluid ◽  
Reference Method ◽  
Prostatic Acid Phosphatase ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

Abstract We describe the development of a stable reference material for prostatic acid phosphatase, derived from human prostatic tissue and human seminal fluid. The enzyme was purified by an L-tartramic acid affinity-chromatography technique. Two-dimensional electrophoresis revealed essentially no contaminating proteins, and specific tests revealed no contaminating enzymes. The preparations, in a matrix containing 30 g of human serum albumin and 0.1 mol of sodium acetate per liter, pH 6.0, were studied with respect to stability of both catalytic activity and immunological identity. We conclude that the preparations from either source are satisfactorily stable, and that either is acceptable for use in preparing clinical reference materials. These materials will be used in developing a reference method.

The properties of acidic compartments in developing schistosomula ofSchistosoma mansoni

Parasitology ◽  
2003 ◽  
Vol 127 (3) ◽  
pp. 253-264 ◽  
Author(s):  
B. H. AL-ADHAMI ◽  
J. THORNHILL ◽  
A. AKHKHA ◽  
M. J. DOENHOFF ◽  
J. R. KUSEL
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Histochemical Staining ◽  
Transformation Process ◽  
Percentage Area ◽  
Red Dye ◽  
Energy Dependent ◽  
Acidic Compartments ◽  
Phosphatase Enzyme

A variety of fluorescent probes have been used to study the acidic compartments in cercariae and schistosomula ofSchistosoma mansoni. Freshly transformed schistosomula treated with the LysoTracker Red dye specific for lysosomes showed large acid-containing compartments (0·5–10 μm in size). The uptake of the dye is an energy-dependent process that depends on the metabolic activity of schistosomula. The compartments were quantified individually with respect to area, quantity of fluorescence and the total number/schistosomulum. Under normal conditions these compartments were not found in untreated cercariae, but appeared in cercariae slightly damaged by poly-L-lysine. The formation of these compartments seemed to be related to the development of cercariae into schistosomula as the number of compartments and uptake of fluorescence increased with time after transformation. Also, the method of transformation as well as thein vitroincubation of the parasite affected the percentage area of compartments/schistosomulum. Acid phosphatase enzyme activity was assessed using an endogenous phosphatase probe. Living and fixed schistosomula displayed the presence of enzyme activity in compartments of the same size and distribution as the acid-rich compartments. This was confirmed by histochemical staining showing deposition of enzyme-generated lead at the sites of phosphatase activity. We suggest that the development of acidic compartments is important during the transformation process or as a consequence of damage.

scholarly journals Thermosensitive Gel Containing Cellulose Acetate Phthalate-Efavirenz Combination Nanoparticles for Prevention of HIV-1 Infection

2015 ◽  
Vol 11 (3) ◽  
pp. 416-427 ◽  
Author(s):  
Abhijit A. Date ◽  
Annemarie Shibata ◽  
Emily Mcmullen ◽  
Krista La Bruzzo ◽  
Patrick Bruck ◽  
...  
Keyword(s):  
Cellulose Acetate ◽  
Cellulose Acetate Phthalate ◽  
Thermosensitive Gel ◽  
Hiv 1 ◽  
Prevention Of Hiv

ACID PHOSPHATASE HYDROLYSIS OF PHOSPHORIC ESTERS

1955 ◽  
Vol 33 (1) ◽  
pp. 539-544 ◽  
Author(s):  
G. E. Delory ◽  
G. S. Wiberg ◽  
Merle Hetherington
Keyword(s):  
Acid Phosphatase ◽  
Seminal Fluid ◽  
Optimum Ph ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

The rate of hydrolysis and optimum pH of hydrolysis of seminal fluid acid phosphatase have been studied for a number of phosphoric esters. As the acidity of the substrate increases there is a tendency for the rate of hydrolysis to increase and for the optimum pH to move farther away from neutrality. The increased rate of hydrolysis of phenol phosphates or of substituted phenol phosphates can not be accounted for by phenolase activity.

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