Physicochemical studies on the characterization of Triton X 100 micelles in an aqueous environment and in the presence of additives

Mandal, Abhijit; Ray, Shannon Joanne; Biswas, Arunangshu; Moulik, Satya P.

doi:10.1021/j100445a012

Cited by 114 publications

(107 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[31]. The increase of all these thermodynamic activation parameters of collagen in buffer as well as in the presence of surfactant additives in the present study have supported the idea that the structure of water in the collagen is ordered.…”

Section: Thermodynamic Parameterssupporting

confidence: 86%

“…Utilizing the phase equilibrium model, the standard free energy change for formation of micelles in buffer may conveniently by written as where (cmc), = cmc in buffer and Yb = activity coefficient of the free species in buffer; the other symbols have their usual significance. Neglecting activity effects [17,26,28,53,541, the cmc values obtained in this study when compared with those in pure buffer can help in evaluating the standard free energy of transfer from buffer (aqueous) to the additive environments thus (AGO),,. = RTln [(CmC)additive/(CmC)bufferl .…”

Section: Micelle Formation and Energy Transfermentioning

confidence: 99%

“…It is generally accepted [31] that the hydration decreases with the increase in temperature in the case of nonionic surfactants and some proteins. We have also observed the same phenomenon [37] in collagens of shark skin, bovine skin, desamido and type-I11 from human placenta (our unpublished results).…”

Section: Hydrated Volume and Interaction Of Surfactant With Collagenmentioning

confidence: 99%

See 2 more Smart Citations

Physico‐chemical studies of micelle formation on sepia cartilage collagen solutions in acetate buffer and its interaction with ionic and nonionic micelles

Mandal

Ramesh

Dhar

1987

European Journal of Biochemistry

View full text Add to dashboard Cite

Sepia cartilage collagen (pepsin-extracted) in acetate buffer (pH = 2.98) forms micelles at a particular concentration below which they do not normally form. The critical micelle concentration (cmc) of the collagen was determined in buffer as well as in SDS, cetyltrimethylammonium bromide (CTAB) and Tween-80 micellar environments at different temperatures. Mutual interaction of collagen micelles with the ionic and nonionic micelles through the formation of the mixed micelle concept has also been found. The cmc of collagen decreased in the presence of SDS and Tween-80 micelles whereas it increased in the presence of CTAB micelles. This clearly suggests that the micelle formation of collagen is facilitated by the presence of SDS and Tween-80 and hindered by CTAB micelles. The various thermodynamic parameters were estimated from viscosity measurements and the transfer of collagen into the micelles of various surfactants and the reverse phenomenon was analyzed. This analysis has also been modelled conceptually as a different phase and the results have supported the above phenomenon. Our thermodynamic results are also able to predict the exact denaturation temperature as well as the structural order of water in the collagen in various environments. The hydrated volumes, Vh, of collagen in the above environments and intrinsic viscosity were also calculated. The low intrinsic viscosity, [?I, of collagen in an SDS environment compared to buffer and other surfactant environments suggested more workable systems in cosmetic and dermatological skin care preparations. The one and two-hydrogen-bonded models of this collagen in various environments have been analyzed. The calculated thermodynamic parameters varied with the concentration of collagen. The change of thermodynamic parameters from coil-coil to random-coil conformation upon denaturation of collagen were calculated from the amount of proline and hydroxyproline residues and compared with viscometric results. Thermodynamic results suggest that the stability of the collagen in the additive environments is in the following order: SDS > Tween-80 > buffer > CTAB.It is well known that the structure of water is important for interactions between proteins and membrane transport phenomena. These interactions are difficult to study due to the fact that the exact shapes, sizes and structure of the proteins are not clearly known. A favourable exception is collagen, consisting of triple-stranded helices which can be regarded as rigid rods. According to X-ray diffraction patterns the rods are packed in a complex lattice [l]. The important features are that the rods are aligned along the fiber axis and that the lattice expands [2] commensurate with the water content. The studies from various sources have indicated that the structure of water absorbed in collagen is different from that of water in bulk. Broad-line NMR measurements [3 -61 have shown two absorption lines instead of one. This may be the reason that the water molecules in collagen do not rotating isotropically. Moreover,...

show abstract

Section: Thermodynamic Parameterssupporting

confidence: 86%

Section: Micelle Formation and Energy Transfermentioning

confidence: 99%

Section: Hydrated Volume and Interaction Of Surfactant With Collagenmentioning

confidence: 99%

See 1 more Smart Citation

Physico‐chemical studies of micelle formation on sepia cartilage collagen solutions in acetate buffer and its interaction with ionic and nonionic micelles

Mandal

Ramesh

Dhar

1987

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

Section: Introductionmentioning

confidence: 99%

“…Polyethylene glycol alkyl ethers have been selected as the nonionic type of surfactant in many studies about mixed micelles (3,9,11,17,19). Only a few studies are relative to properties of TX-100 mixed micelles (10,14,19). Recently, we have found that cetyltrimethylammonium bromide (CTAB) and TX-100 molecules are uniformly arranged in the mixed micellar core with the polar head of CTAB situated between the first ethoxy groups next to the phenoxy rings of TX-100 (20).…”

Section: Introductionmentioning

confidence: 99%

1H NMR Study of Mixed Micellization of Sodium Dodecyl Sulfate and Triton X-100

Wang

Mao

Miao

et al. 2001

Journal of Colloid and Interface Science

View full text Add to dashboard Cite

Solution properties of methyl methacrylate–acrylonitrile copolymers

Asaduzzaman

Rakshit

Devi

1993

J of Applied Polymer Sci

View full text Add to dashboard Cite

SYNOPSISCharacterization of methyl methacrylate-acrylonitrile copolymers is done through viscosity, swelling, and differential refractometric studies. Viscosities of the copolymers and homopolymers were determined at 30,40, and 5OoC. The activation parameters of viscous flow, voluminosity, and shape factor were also calculated. The average shape factor was observed to be 2.5 ? 0.005 for all copolymer systems. Viscosity molecular weights were calculated, and from intramolecular expansion factor (a), it was observed that copolymers are less flexible than are homopolymers. d n / dc values obtained from differential refractometry are in good agreement with those calculated theoretically. 0 1993 John Wiley & Sons, Inc.

show abstract

Physicochemical studies on the characterization of Triton X 100 micelles in an aqueous environment and in the presence of additives

Cited by 114 publications

References 9 publications

Physico‐chemical studies of micelle formation on sepia cartilage collagen solutions in acetate buffer and its interaction with ionic and nonionic micelles

Physico‐chemical studies of micelle formation on sepia cartilage collagen solutions in acetate buffer and its interaction with ionic and nonionic micelles

1H NMR Study of Mixed Micellization of Sodium Dodecyl Sulfate and Triton X-100

Solution properties of methyl methacrylate–acrylonitrile copolymers

Contact Info

Product

Resources

About