Surface Characterization of Soap-Free Carboxylated Polymer Latices

Shirahama, Hiroyuki; Suzawa, Toshiro

doi:10.1295/polymj.16.795

Cited by 26 publications

(17 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These steps probably reflect a conformational rearrangement of adsorbed BSA molecules [2,4,[6][7][8] rather than a multilayer adsorption. The maximum plateau value for every latex is obtained in the neighborhood of the IEP of BSA, i. e., at pH 5.0.…”

Section: Adsorption #Othermsmentioning

confidence: 99%

See 1 more Smart Citation

Adsorption of bovine serum albumin onto styrene/acrylic acid copolymer latex

Shirahama

Suzawa

1985

Colloid & Polymer Sci

View full text Add to dashboard Cite

The adsorbability of bovine serum albumin (BSA) onto styrene/acrylic acid copolymer (PS/PAA) latex prepared without emulsifier was investigated as a function of pH and ionic strength. Polystyrene (PS) latex was used as a reference sample. The adsorption isotherms of BSA onto PS/PAA latices showed a stepwise nature. The thickness of the adsorbed BSA monolayer suggested that BSA molecules adsorbed onto PS/PAA2 latex (here, the subscript, i. e., 2, represents the tool % of acrylic acid used in copolymerization) in a "side-on" mode near the isodectric point (IEP) of this protein. However, in the case of PS/PAAs latex, a portion of the BSA molecules probably adsorbed in a "loop" or an "end-on" mode. The amount of BSA adsorbed onto PS/PAA latices greatly depended on pH and ionic strength; its value showed a maximum in the neighborhood of the IEP of BSA as in PS latex. The amount adsorbed onto PS/PAA latices except in the alkaline pH region was greater than that onto PS latex. Moreover, the amount adsorbed onto PS/PAA 5 latex was greater than that onto PS/PAA2 latex. Both these results are probably attributed to hydrogen bonding between BSA molecule and PS/PAA latex. It was found that the adsorbability of BSA especially at a high ionic strength greatly depended on the surface properties of polymer latices.

show abstract

Section: Adsorption #Othermsmentioning

confidence: 99%

“…We also, hitherto, have studied the adsorbability of bovine serum albumin (BSA) onto various polymer latices as a function of pH and ionic strength etc. [5][6][7][8]. As a result, it was found that BSA adsorption depended upon not only electrostatic interactions but also surface properties of latices.…”

Section: Introductionmentioning

confidence: 99%

Adsorption of bovine serum albumin onto styrene/acrylic acid copolymer latex

Shirahama

Suzawa

1985

Colloid & Polymer Sci

View full text Add to dashboard Cite

show abstract

“…In recent years, much attention has been paid to the use of proteins conjugated to polymer colloids in biomedical applications (Lukowski et al, 1992;Rembaum et al, 1976;Shirahama and Suzawa, 1984;Suzawa et al, 1982Suzawa et al, , 1983. Such colloids are easy to produce and can be prepared with a high degree of monodispersity (Bale et al, 1989;Ceska, 1974a,b;Sakota and Okaya, 1976).…”

Section: Introductionmentioning

confidence: 99%

Charge‐directed targeting of antimicrobial protein‐nanoparticle conjugates

Satishkumar

Vertegel

2008

Biotech & Bioengineering

View full text Add to dashboard Cite

Use of antimicrobial enzymes covalently attached to nanoparticles is of great interest as an antibiotic-free approach to treat microbial infections. Intrinsic properties of nanoparticles can also be used to add functionality to their conjugates with biomolecules. Here, we show in a model system that nanoparticle charge can be used to enhance delivery and increase bactericidal activity of an antimicrobial enzyme, lysozyme. Hen egg lysozyme was covalently attached to two types of polystyrene latex nanoparticles: positively charged, containing aliphatic amine surface groups, and negatively charged, containing sulfate and chloromethyl surface groups. In the case of bacterial lysis assay with a Gram-positive bacteria Micrococcus lysodeikticus, activity of lysozyme conjugated to positively charged nanoparticles was approximately twice as large as that of free lysozyme, while lysozyme conjugated to negatively charged nanoparticles showed little detectable activity. At the same time, when assayed using a low-molecular weight oligosaccharide substrate, lysozyme attached to both positively and negatively charged nanoparticles showed slightly lower activity than free enzyme. A possible explanation of these results is that lysozyme attached to negatively charged nanoparticles cannot be effectively targeted to the bacteria because of the electrostatic Coulombic repulsion from the negatively charged bacterial cell walls, whereas lysozyme conjugated to positively charged nanoparticles was targeted better than free enzyme due to stronger electrostatic attraction to bacteria. Zeta potential measurements confirmed the validity of this hypothesis. Thus, nanoparticle charge is an important factor that can be used to control targeting and activity of protein-nanoparticle conjugates.

show abstract

“…The results reported here are in agreement with other reported studies in the literature. 23,24 Adsorption of BSA.…”

Section: Resultsmentioning

confidence: 99%