Lysozyme binding to poly(4-vinyl-N-alkylpyridinium bromide).
The adsorption behavior of polycations at ionic strengths (I) ranging from 0.001 to 0.1 onto silicon wafers was studied by means of ellipsometry, contact angle measurements and atomic force microscopy (AFM). Polycations chosen were bromide salts of poly(4-vinylpyridine) N-alkyl quaternized with linear aliphatic chains of 2 and 5 carbon atoms, QPVP-C2 and QPVP-C5, respectively. Under I=0.001 the reduction of screening effects led to low adsorbed amounts of QPVP-C2 or QPVP-C5 (1.0+/-0.1 mg/m(2)), arising from the adsorption of extended chains. Upon increasing I to 0.1, screening effects led to conformational changes of polyelectrolyte chains in solution and to higher adsorbed amount values (1.9+/-0.2 mg/m(2)). Advancing contact angle theta(a) measurements performed with water drops onto QPVP-C2 and QPVP-C5 adsorbed layers varied from (45+/-2) degrees to (50+/-5) degrees, evidencing the exposure of both hydrophobic alkyl groups and charged moieties. The adsorption of lysozyme (LYZ) molecules to QPVP-C5 layers was more pronounced than to QPVP-C2 films. Antimicrobial effect of LYZ bound to QPVP-C2 or QPVP-C5 layers or to Si wafers was evaluated with enzymatic assays using Micrococcus luteus as substrates. The adsorption behavior of QPVP-C2 and QPVP-C5 at the water-air interface was studied by means of surface tension measurements. Only QPVP-C5 was able to reduce water surface tension. Mixtures of LYZ and QPVP-C5 were more efficient in reducing surface tension than pure LYZ solution, evidencing co-adsorption at liquid-air interface. Moreover, antimicrobial action observed for mixtures of LYZ and QPVP-C5 was more pronounced than that measured for pure LYZ. Hydrophobic interaction between LYZ and QPVP-C5 in solution seems to drive the binding and to preserve LYZ secondary structure.
Silva
Rubens A
RA
Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.
Urzúa
Marcela D
MD
Petri
Denise F S
DF
D000327:Adsorption; D002412:Cations; D057927:Hydrophobic and Hydrophilic Interactions; D018625:Microscopy, Atomic Force; D008968:Molecular Conformation; D009113:Muramidase / Q000737:chemistry*; D011073:Polyamines / Q000737:chemistry; D000071228:Polyelectrolytes; D011145:Polyvinyls / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013500:Surface Tension
D002412:Cations; D009113:Muramidase; D011073:Polyamines; D000071228:Polyelectrolytes; D011145:Polyvinyls; C019535:poly(4-vinylpyridine)