Influence of urea additives on micellar morphology/protein conformation.
The present study highlights the fact that the effect of additives (urea, monomethylurea, thiourea) on the supramolecular assemblies and proteins is strikingly similar. To investigate the effect, a viscometeric study on sphere-to-rod transition (s-->r) was undertaken in a system (3.5% tetradecyltrimethylammonium bromide+0.05 M NaBr + 1-pentanol [P.M. Lindemuth, G.L. Bertand, J. Phys. Chem. 97 (1993) 7769]) in the presence and absence of the said additives. [1-pentanol] needed for s-->r (i.e. [1-pentanol]s-->r) was determined from the relative viscosity versus [1-pentanol] profiles. It was observed that the additives preponed as well as postponed s-->r depending upon their nature and concentrations. These effects are explained in terms of increased polarity of the medium and the adsorption ability of urea/monomethylurea on the charged surfactant monomers of the micelle. In case of thiourea, postponement of s-->r was observed throughout which is attributed to its structure. To derive an analogy between micelles and proteins the additive-induced conformational changes of the protein, bovine serum albumin (BSA) was taken to monitor secondary structural changes and tryptophanyl fluorescence. A marked increase in secondary structure (far-UVCD) and increased tryptophanyl fluorescence with a marked blue shift in lambdamax was observed in presence of low concentrations of urea or alkylurea. This indicates that a more compact environment is created in presence of these additives, if added judiciously. Addition of thiourea to BSA caused a marked quenching without any significant change in lambdamax. The large decrease in tryptophanyl emission in presence of low thiourea concentrations seems to be specific and related to thiourea structure as no corresponding changes were observed in urea/alkylurea. All these effects pertaining to protein behavior fall in line with that of morphological observations on the present as well as surfactant systems studied earlier [S. Kumar, N. Parveen, Kabir-ud-Din, J. Phys. Chem. B 108 (2004) 9588].
Gull
Nuzhat
N
Department of Chemistry, Aligarh Muslim University, Aligarh 202 002, India.
Kumar
Sanjeev
S
Ahmad
Basir
B
Khan
Rizwan Hassan
RH
Kabir-ud-Din
D000818:Animals; D002021:Buffers; D002417:Cattle; D002942:Circular Dichroism; D004305:Dose-Response Relationship, Drug; D005260:Female; D006863:Hydrogen-Ion Concentration; D008782:Methylurea Compounds / Q000494:pharmacology; D008823:Micelles; D011487:Protein Conformation / Q000187:drug effects*; D017433:Protein Structure, Secondary / Q000187:drug effects; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D012995:Solubility; D013050:Spectrometry, Fluorescence; D013890:Thiourea / Q000494:pharmacology; D014364:Tryptophan / Q000737:chemistry; D014508:Urea / Q000494:pharmacology*; D014783:Viscosity; D014867:Water / Q000737:chemistry
D002021:Buffers; D008782:Methylurea Compounds; D008823:Micelles; D014867:Water; D012710:Serum Albumin, Bovine; D014364:Tryptophan; D014508:Urea; D013890:Thiourea; C002352:methylurea