Interaction of a bovine serum albumin (BSA) protein with mixed anionic–cationic surfactants and the resultant structure

نویسندگان

چکیده

The interaction of a bovine serum albumin (BSA) protein with the mixture anionic sodium dodecyl sulfate (SDS) and cationic dodecyltrimethylammonium bromide (DTAB) has been investigated by small-angle neutron scattering (SANS) dynamic light (DLS).

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

Optical and Nano structural properties of Hematite (α-Fe2O3) nanorods in interaction with Bovine Serum Albumin (BSA) Protein Solution

Hematite (α-Fe2O3) nanorods were synthesized by hydrothermal method using Cetyltrimethylammonium bromide (CTAB) as a surfactant agent. To study optical, nanostructural properties, and to control the morphology and shape of nanorods, 0.025 mol L-1, 0.05 mol L-1 and 0.1 mol L-1 concentration of CTAB were used. Moreover, the effect of interaction between bovine serum albumin (BSA) A9418-5G protein...

متن کامل

Interaction of Phthalocyanine with Egg albumin and Bovine serum albumin

The interaction of bovine serum albumin ( BSA) and egg albumin with water solublephthalocyanine, cobalt (ΙΙ) 4, 4′ , 4′′, 4′′′- tetrasulfophthalocyanine ( CoTSPc) , has been studiedby the UV- Vis method at pH 7.0 and five different temperatures 20, 25, 30, 35 and 40°C. Theformation constants have been elucidated by using spectrophotometric titration and computerSQUAD program data refinement. Th...

متن کامل

The interaction between bovine serum albumin and surfactants.

1. Potassium n-decyl phosphate binds exothermically to bovine serum albumin at pH 7.0 to form a specific complex containing approx. 60 phosphate anions. 2. The formation of the complex is accompanied by changes in the u.v. difference spectrum of the protein. 3. At higher phosphate concentrations (above 0.4mM) surfactant molecules continue to be bound, and the protein undergoes a gross change in...

متن کامل

Photocontrol of protein folding: the interaction of photosensitive surfactants with bovine serum albumin.

The photoresponsive interaction of light-sensitive azobenzene surfactants with bovine serum albumin (BSA) at neutral pH has been investigated as a means to control protein folding with light irradiation. The cationic azobenzene surfactant undergoes a reversible photoisomerization upon exposure to the appropriate wavelength of light, with the visible-light (trans) form of the surfactant being mo...

متن کامل

interaction of phthalocyanine with egg albumin and bovine serum albumin

the interaction of bovine serum albumin ( bsa) and egg albumin with water solublephthalocyanine, cobalt (ιι) 4, 4′ , 4′′, 4′′′- tetrasulfophthalocyanine ( cotspc) , has been studiedby the uv- vis method at ph 7.0 and five different temperatures 20, 25, 30, 35 and 40°c. theformation constants have been elucidated by using spectrophotometric titration and computersquad program data refinement. th...

متن کامل

ذخیره در منابع من


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

ژورنال

عنوان ژورنال: Soft Matter

سال: 2021

ISSN: ['1744-683X', '1744-6848']

DOI: https://doi.org/10.1039/d1sm00264c