studying the stability of s-layer protein of lactobacillus acidophilus atcc 4356 in simulated gastrointestinal fluids using sds-page and circular dichroism

نویسندگان

neda eslami 1- department of pharmaceutics, school of pharmacy, shahid beheshti university of medical sciences, tehran, iran. 2- department of biology, school of sciences, alzahra university of basic sciences, tehran, iran.

rouha kasra kermanshahi department of biology, school of sciences, alzahra university of basic sciences, tehran, iran.

mohammad erfan department of pharmaceutics, school of pharmacy, shahid beheshti university of medical sciences, tehran, iran.

چکیده

crystalline arrays of proteinaceous subunits forming surface layers (s-layers) are now recognized as one of the most common outermost cell envelope components of prokaryotic organisms. the surface layer protein of lactobacillus acidophilus atcc4356 is composed of a single species of protein of apparent molecular weight of 43-46 kda. considering the lactobacillus acidophilus atcc4356 having the s-layer is stable in harsh gastrointestinal (gi) conditions, a protective role against destructive gi factors which has been proposed for these nanostructures. it opens interesting perspectives in the using and development of this s-layer as a protective coat for oral administration of unstable drug nanocarriers. to achieve this goal, it is necessary to study the in-vitro stability of the s-layers in the simulated gastrointestinal fluids (sgif). this study was planned to evaluate the in-vitro stability of the extracted s-layer protein of lactobacillus acidophilus atcc4356 in sgif using it as a protective coat in oral drug delivery. sodium dodecyl sulfate gel electrophoresis (sds-page) and circular dichroism (cd) spectroscopy were used to study the stability of the s-layer protein incubated in sgif. both the sds-page and cd spectra results showed that lactobacillus acidophilus atcc4356 s-layer protein is stable in simulated gastric fluid (sgf) with ph = 2 up to 5 min. it is stable in sgf ph = 3.2 and above it, with and without pepsin. it is also stable in all the simulated intestinal fluids. this s-layer is also stable in all of the simulated intestinal fluids.

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Studying the Stability of S-Layer Protein of Lactobacillus Acidophilus ATCC 4356 in Simulated Gastrointestinal Fluids Using SDS-PAGE and Circular Dichroism

Crystalline arrays of proteinaceous subunits forming surface layers (S-layers) are now recognized as one of the most common outermost cell envelope components of prokaryotic organisms. The surface layer protein of Lactobacillus acidophilus ATCC4356 is composed of a single species of protein of apparent molecular weight of 43-46 KDa. Considering the Lactobacillus acidophilus ATCC4356 having the ...

متن کامل

Studying the Stability of S-Layer Protein of Lactobacillus Acidophilus ATCC 4356 in Simulated Gastrointestinal Fluids Using SDS-PAGE and Circular Dichroism

Crystalline arrays of proteinaceous subunits forming surface layers (S-layers) are now recognized as one of the most common outermost cell envelope components of prokaryotic organisms. The surface layer protein of Lactobacillus acidophilus ATCC4356 is composed of a single species of protein of apparent molecular weight of 43-46 KDa. Considering the Lactobacillus acidophilus ATCC4356 having the ...

متن کامل

Studying the Stability of S-Layer Protein of Lactobacillus Acidophilus ATCC 4356 in Simulated Gastrointestinal Fluids Using SDS-PAGE and Circular Dichroism

Crystalline arrays of proteinaceous subunits forming surface layers (S-layers) are now recognized as one of the most common outermost cell envelope components of prokaryotic organisms. The surface layer protein of Lactobacillus acidophilus ATCC4356 is composed of a single species of protein of apparent molecular weight of 43-46 KDa. Considering the Lactobacillus acidophilus ATCC4356 having the ...

متن کامل

Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356.

We describe a new enzymatic functionality for the surface layer (S-layer) of Lactobacillus acidophilus ATCC 4356, namely, an endopeptidase activity against the cell wall of Salmonella enterica serovar Newport, assayed via zymograms and identified by Western blotting. Based on amino acid sequence comparisons, the hydrolase activity was predicted to be located at the C terminus. Subsequent clonin...

متن کامل

Inhibition of H9N2 Virus Invasion into Dendritic Cells by the S-Layer Protein from L. acidophilus ATCC 4356

Probiotics are essential for the prevention of virus invasion and the maintenance of the immune balance. However, the mechanism of competition between probiotics and virus are unknown. The objectives of this study were to isolate the surface layer (S-layer) protein from L. acidophilus ATCC 4356 as a new antiviral material, to evaluate the stimulatory effects of the S-layer protein on mouse dend...

متن کامل

منابع من

با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید


عنوان ژورنال:
the iranian journal of pharmaceutical research

جلد ۱۲، شماره Supplement، صفحات ۴۷-۵۶

میزبانی شده توسط پلتفرم ابری doprax.com

copyright © 2015-2023