A systematic study of bovine serum albumin (BSA) and sodium dodecyl sulfate (SDS) interactions by surface tension and small angle X-ray scattering

Classical parameters obtained from surface tension technique coupled to small angle X-ray scattering (SAXS) measurements gave support to investigate conformational changes in the bovine serum albumin (BSA)-sodium dodecyl sulfate (SDS) complexes, as well as the size of the micelle-like clusters distributed along the polypeptide chain. The studied systems were composed of 1 wt% of BSA in the absence and presence of increasing SDS molar concentration up to 80 mM, under experimental conditions of low ionic strength and pH 5.40. At SDS concentrations below the critical aggregation concentration (cac) of 2.2 mM, SAXS results indicate that the detergent does not modify the native protein conformation. However, the beginning of protein unfolding, evidenced by SAXS through an increase in the values of radius of gyration Rg and protein maximum dimension Dmax, is coincident with the onset of SDS cooperative binding to BSA identified by the first breakpoint in the surface tension-SDS profile. Further SDS addition leads to the formation of micelle-like aggregates randomly distributed along the unfolded polypeptide chain, consistent to a necklace and bead model. The SAXS data also demonstrate that the SDS micelles grow in size up to 50 mM detergent. At 50 mM surfactant, the micelles stop growing. This concentration is near the BSA saturation binding by SDS measured by dialyzes and indicated by the second breakpoint in surface tension-SDS profile. The SAXS and surface tension data are also consistent with the formation of free micelles in equilibrium with BSA-SDS complexes for surfactant amount above the saturation.     

Study on the interactions of kaempferol and quercetin with intravenous immunoglobulin by fluorescence quenching, fourier transformation infrared spectroscopy and circular dichroism spectroscopy

The interactions of kaempferol and quercetin with intravenous immunoglobulin (IVIG) were studied in vitro by spectroscopic methods including fluorescence spectra, Fourier transformation infrared (FT-IR) spectra and circular dichroism (CD) spectra. The binding parameters for the reactions calculated according to the Sips equation suggested that the bindings of IVIG to kaempferol and quercetin were characterized by two binding sites with the average affinity constants K(o) at 1.032 x 10(4) M(-1) and 1.849 x 10(4) M(-1), respectively. The binding of IVIG with quercetin is stronger than that of IVIG with kaempferol. They were of non-specific and weak drug-protein interactions. Docking was used to calculate the interaction modes between kaempferol and quercetin with IVIG. The secondary structural compositions of free IVIG and its kaempferol, quercetin complexes were calculated by the FT-IR difference spectra, self-deconvolution, second derivative resolution enhancement and the curve-fitting procedures of amide I band respectively, which are in good agreement with the analyses of CD spectra. The effect of 3'-OH substituent in quercetin is distinct between the interactions of IVIG with kaempferol and quercetin for the secondary structure of the protein. The observed spectral changes indicate a partial unfolding of the protein structure, but the typical beta structural conformation of IVIG is still retentive in the presence of both drugs in aqueous solution. The average binding distances between the chromophores of IVIG with kaempferol (4.30 nm) and quercetin (4.35 nm) were obtained on the basis of the theory of F?rster energy transfer. IVIG can serve as transport protein (carrier) for kaempferol and quercetin.     

Synthesis,Characterization, Structural Description,Micellization Behavior,DNA Binding Study and Antioxidant Activity of 4, 5 and 6-Coordinated Copper(II) and Zinc(II) Complexes

Four mononuclear copper(II) and zinc(II) complexes were synthesized by the reaction of copper and zinc salts with 3,4-dichlorophenylactic acid, 2-bromophenylactic acid, biphenylacetic acid (O-donor ligand) and bipyridine (N-donor ligands) having the general formulae [(L)₂Cu(bp)(H₂O)] ( 1 ), [(BpA)₂Cu(bp)] ( 2 ), [(L)₂Zn(bp)(H₂O)] ( 3 ) and [(L*)₂Zn(bp)] ( 4 ) (L = 3,4-dichlorophenylacetate, L* = 2-bromophenylacetate bp = bipyridine, and BpA = biphenylacetate). Structures of all compounds were characterized through FT-IR spectroscopy and X-ray diffraction analysis. FT-IR spectra of all complexes confirmed the binding mode of Cu-O and Zn-O. XRD data revealed that complexes 1 – 3 exhibited distorted octahedral arrangement, whereas complex 4 has a distorted tetrahedral environment. Micellization behavior was examined with anionic surfactant (SDS) by conductance measurement as well as absorption spectral analysis. DNA binding study was assessed through viscosity measurement and UV/Vis spectrophotometry. DPPH free radical scavenging assay was measured by UV/Vis spectrophotometry. The results showed nice biological potential of all the complexes.     

Interaction of water-soluble cationic porphyrin with anionic surfactant

The interaction of a cationic water-soluble porphyrin, 5,10,15,20-tetrakis [4-(3-pyridiniumpropoxy)phenyl]porphyrin tetrakisbromide (TPPOC3Py), with anionic surfactant, sodium dodecyl sulfate (SDS), in aqueous solution has been studied by means of UV-vis, (1)H NMR, fluorescence, circular dichroism (CD) spectra and dynamic laser light scattering (DLLS), and it reveals that TPPOC3Py forms porphyrin-surfactant complexes (aggregates), including ordered structures J- and H-aggregates, induced by association with surfactant monomers below the SDS critical micelle concentration (cmc), and forms micellized monomer upon the cmc, respectively. The position of TPPOC3Py in the micelle is determined, which is not in the micelle core instead of intercalated among the SDS chains, most likely with the pyridinium group extending into the polar headgroup region of the micelle.     

A capillary electrophoresis study on the influence of beta-cyclodextrin on the critical micelle concentration of sodium dodecyl sulfate

The influence of beta-cyclodextrin (beta-CD) on the critical micelle concentration (CMC) of sodium dodecyl sulfate (SDS) was investigated by capillary electrophoresis using anionic chlorophenols as probe molecules at pH 7.0. The variations of the electrophoretic mobility of probe molecules as a function of surfactant concentration in both premicellar and micellar regions in the absence and presence of beta-CD was analyzed. The results indicate that, as a consequence of a strong inclusion complexation between beta-CD and SDS, the encapsulation of beta-CD with probe molecules is greatly diminished, or even vanished, in the presence of SDS. The complexes formed between beta-CD and SDS monomers exist predominantly in the form of a 1:1 stoichiometry, while the complexes with a 2:1 stoichiometry reported previously in the literature as a minor component may exist by less than 10%. The elevation of the CMC value of SDS depends not only on the concentration of beta-CD in the buffer electrolyte but also on methanol content in the sample solution. The binding constants of probe molecules to beta-CD, to surfactant molecules, and to the complexes formed between beta-CD and SDS are reported.     

A foldamer-based chiroptical molecular switch that displays complete inversion of the helical sense upon anion binding

Chiral indolocarbazole dimers fold into a helical conformation by virtue of intramolecular hydrogen bonds, as demonstrated by (1)H NMR and CD spectra and optical rotations. In particular, the optical properties of the dimers were found to be extremely sensitive to the nature of the solvent, depending on whether they are folded or not. The helical sense of the dimers can be reversibly switched by binding sulfate ion, which gives rise to complete inversion of the CD spectra. The binding mode and absolute stereochemistry of the sulfate complexes was unequivocally determined by single-crystal X-ray structures, which are all consistent with the CD and (1)H NMR spectra in solution.     

Interactions between carbonic anhydrase and its inhibitors revealed by gel electrophoresis and circular dichroism

Structural properties, and especially the differential stability, of complexes between carbonic anhydrase (CA) and three sulfonamide inhibitors, acetazolamide, dorzolamide and methazolamide, were investigated by spectroscopic and electrophoretic techniques. These included denaturant gradient gel electrophoresis either across a urea or a steady-state transverse sodium dodecyl sulfate (SDS) gradient. Acetazolamide, the smallest and most hydrophilic of the sulfonamides, forms the most stable complex in the presence of urea, whereas dorzolamide, with a bulky and hydrophobic structure, is most stable against the effects of SDS. At pH 7.4, complexes with dorzolamide show minimal changes in mobility across the SDS gradient, as if unaffected by the detergent, both in the presence and in the absence of excess ligand in the gel. When bound to both acetazolamide and methazolamide, on the other hand, CA displays an increase in mobility above 0.05% SDS, lower in the presence than in the absence of excess ligand. The finding of a distinct pattern for the unliganded enzyme, however, suggests the complexes can still retain the ligand, although binding of the surfactant changes their charge density. Under saturating conditions and in the presence of SDS, the surface charge of all complexes is much lower than for unliganded, denatured CA. Circular dichroism (CD) spectra clearly indicate that the increase in secondary structure and the decrease in tertiary structure brought about in CA by the presence of low concentrations of SDS are largely prevented by complexing with the inhibitors. These observations point out peculiar properties of each CA inhibitor, of potential value in the definition of their biological activities and also in the potential development of novel antagonist molecules.     

Stereoselective bile pigment binding to polypeptides and albumins: a circular dichroism study

Stereoselective recognition of bilirubin and biliverdin by poly(L-lysine) (PLL), poly(D-lysine) (PDL), and poly(L-arginine) (PLA) and their micelles with dodecanoate ions (C(12)) at different pH has been studied using a combination of vibrational and electronic circular dichroism. Biliverdin has been found to be more sensitive to pH in its complexes with the polypeptides. In acidic media in the complexes with PLL-C(12) and PDL-C(12) the conformation becomes more closed than the characteristic one found at physiological pH. Partial flattening and chiral self-association of bilirubin molecules takes place at higher concentrations with PLL and PDL. For both pigments, inversions of the ECD signals are observed in the systems with PLA at pH > or = 8.5. This study was carried out in order to clarify the role of Lys and Arg residues in pigment binding to serum albumin. The circular dichroism spectra obtained for bilirubin bound to different mammalian serum albumins have been compared with the homology within the IIA principal ligand-binding structural domains. Analysis suggests that the chiroptical properties of the pigment in the complexes with serum albumins depend on the location of Lys and/or Arg at positions 222 and 199 in the binding site.     

Effects of SDS on the sol–gel transition of konjac glucomannan in SDS aqueous solutions

The interaction between konjac glucomannan (KGM) and an anionic surfactant, sodium dodecyl sulfate (SDS) is studied by rheological, circular dichroism (CD), conductivity, electron spin resonance (ESR), and FT-IR measurements. Since KGM is a neutral polysaccharide and has no significant hydrophobic side groups, the critical micelle concentration value of SDS is not influenced with the addition of KGM, and no marked binding occurs between them. SDS makes no conformational changes of KGM with or without heat treatment. The weak alkaline character of SDS induces the deacetylation of KGM chains and makes it form gels with heat treatment. At the same pH value, the gelation time needed for KGM by using SDS as the coagulant is shorter than that by using Na₂CO₃. The addition of SDS promotes the gelation process of KGM, indicating that although the interaction is weak, SDS micelles seem to play an important role in the gelation of KGM.     

Interaction of unfolded lysozyme with hexa(oxyethylene) dodecylether

Reduced lysozyme at pH 2.5 bound hexa(oxyethylene) dodecylether in two steps and the bound amount of the surfactant reached as much as 0.5–0.6 mole per mole amino acid residue in the cooperative binding step. Circular dichroism (CD) spectra suggested a change in the polypeptide main-chain conformation as a result of the surfactant binding, but little or no organization of the tertiary structure. The interaction most likely took place between the hydrocarbon tail of the surfactant and the hydrophobic domain of reduced lysozyme. Alkylated lysozyme, obtained from the reaction with iodoacetamide, gave an essentially identical binding isotherm to that of reduced lysozyme, but different CD results were obtained for each of them.This research was partially supported by a grant-in-aid for scientific research (No. 02403004) from the Ministry of Education, Science, and Culture, Japan, and also by Nippon Oil & Fats Co., Ltd.     

Interaction between casein and sodium dodecyl sulfate

The interaction of the anionic surfactant sodium dodecyl sulfate (SDS) with 2.0 mg/ml casein was first investigated using isothermal titration calorimetry (ITC), dynamic light scattering (DLS), and fluorescence spectra. ITC results show that individual SDS molecules first bind to casein micelles by the hydrophobic interaction. The micelle-like SDS aggregate is formed on the casein chains when SDS concentration reaches the critical aggregation concentration (c1), which is far below the critical micellar concentration (cmc) of SDS in the absence of casein. With the further increase of SDS concentration to the saturate binding concentration c2, SDS molecules no longer bind to the casein chains, and free SDS micelles coexist with casein micelles bound with SDS aggregates in the system. DLS results show that the addition of SDS leads to an increase in the hydrodynamic radius of casein micelles with bound surfactant at SDS concentration higher than 4 mM, and also an increase in the casein monomer molecule (or submicelles) at SDS concentration higher than 10 mM. Fluorometric results suggest the addition of SDS leads to some changes in the binding process of hydrophobic probes to casein micelles.     

Affinity of the anthracycline antitumor drugs Doxorubicin and Sabarubicin for human telomeric G-quadruplex structures

Combining various techniques in solution we proved that Doxorubicin, also called Adriamycin, and Sabarubicin, also known as MEN 10755, bind to the human telomeric sequence, 5'-d[GGG(TTAGGG)(3)]-3' (21-mer), assuming a G-quadruplex structure in the presence of K(+). Complexes of drugs with the 21-mer in 1?:?1 and 2?:?1 stoichiometry coexist in solution. Association constants were obtained from titration experiments and confirmed by isothermal titration calorimetry. The fluorescence of the drugs was quenched upon complexation. UV circular dichroism (CD) spectra of the complexes were characterized by the G-quadruplex signal and indicated that drug binding influences the equilibrium between quadruplex conformations. The visible CD spectra were exclusively due to the drug and show differences in the complexation modes of the two drugs. Spectroscopic and thermodynamic parameters of the 1?:?1 complexes point to drug stacking with the G-quadruplex top or bottom tetrad. Thermodynamic data suggests that the binding of the second drug molecule in the 2?:?1 complex may occur in a groove. Complexation caused a small increase in the thermal stability of the G-quadruplex main conformation, shifting T(m) from 62 to 67 °C.     

Binding of sodium dodecyl sulfate to linear and star homopolymers of the nonionic poly(methoxyhexa(ethylene glycol) methacrylate) and the polycation poly(2-(dimethylamino)ethyl methacrylate): electromotive force, isothermal titration calorimetry, surface tension, and small-angle neutron scattering measurements

We investigated the binding of sodium dodecyl sulfate (SDS) to various linear and star polymers of the nonionic methoxyhexa(ethylene glycol) methacrylate (PMHEGMA) and the ionic 2-(dimethylamino)ethyl methacrylate (PDMAEMA), the latter being a polycation at low pH. The dodecyl sulfate ion selective electrode (EMF), isothermal titration calorimetry (ITC), and surface tension (ST) were applied to gain detailed information about interactions. In all cases there is evidence of significant binding of SDS over an extensive SDS concentration range spanning from ca. 10(-6) to 0.1 mol dm(-3). At pH 3, the polymer PDMAEMA is a strong polycation and here the binding is dominated by electrostatic 1:1 charge neutralization with the anionic surfactant. At their natural pH of 8.6, PMHEGMA and PDMAEMA polymers are essentially nonionic and bind SDS in the form of polymer-bound aggregates in the concentration range of ca. 1 x 10(-3) to 3 x 10(-2) mol dm(-3). All the polymers also bind SDS to a lesser extent at concentrations below 1 x 10(-3) mol dm(-3) reaching as low as 10(-7) mol dm(-3). This low concentration binding process involves the polymer and nonassociated SDS monomers. As far as we are aware, this is the first example that such a low concentration noncooperative binding process could be observed in SDS/neutral polymer systems by EMF and ST. We also showed that the nonionic surfactant hexa(ethylene glycol) mono-n-dodecyl ether (C12EO6) and the cationic cetyltrimethylammonium bromide (C16TAB) interact with star PDMAEMA. We believe that the interaction of C12EO6 and CTAB is of similar noncooperative type as the first SDS binding process in the range from ca. 10(-5) to 0.3 x 10(-3) mol dm(-3). At the high concentration binding limit Csat of SDS, the above polymers become fully saturated with bound SDS micelles. We applied small angle neutron scattering (SANS) to determine the structure and aggregation numbers of the star polymer/bound SDS micelles and calculated the stoichiometry of such supramolecular complexes. The SANS data on PDMAEMA star polymers in the presence of C12EO6 showed only a limited monomer binding in contrast to linear PDMAEMA, which showed monomer C12EO6 binding at low concentrations but micellar aggregates at 6 x 10(-3) mol dm(-3).     

Binding of the bioactive component daphnetin to human serum albumin demonstrated using tryptophan fluorescence quenching

Daphnetin (7,8-dihydroxycoumarin), one of the major bioactive components isolated from Daphne koreane Nakai, has been used in traditional Chinese medicine for the treatment of coagulation disorders. It is also a chelator, an antioxidant and a protein kinase inhibitor. In this paper, a combination of intrinsic fluorescence, Fourier transform infrared (FT-IR) spectroscopy and circular dichroic (CD) spectroscopy has been used to characterize the binding between daphnetin and human serum albumin (HSA) under physiological conditions with drug concentrations of 6.7 x 10(-6) - 2.3 x 10(-5) mol x L(-1), and a HSA concentration of 1.5 x 10(-6) mol x L(-1). Changes in the CD spectra and FT-IR spectra were observed upon ligand binding, and the degree of tryptophan fluorescence quenching did change significantly in the complexes. These data have proved the change in protein secondary structure accompanying ligand binding. The change in tryptophan fluorescence intensity was used to determine the binding constants. The thermodynamic parameters, the enthalpy change (DeltaH) and the entropy change (DeltaS) were calculated to be -12.45 kJ x mol(-1)and 52.48 J x mol(-1) x K(-1) according to the van't Hoff equation, which indicated that hydrophobic and electrostatic interactions played the main role in the binding of daphnetin to HSA, in accordance with the results of calculations performed on a Silicon Graphics Ocatane2 workstation. In addition, the binding distance between daphnetin and HSA was obtained (4.02 nm) based on the Forster energy transfer theory.     

Dibenzodiaza-30-crown-10-appended bis(zinc porphyrin) tweezers: synthesis and crown-assisted chiroptical behaviour

In our program for developing chirality manipulation systems, we synthesized bis(zinc porphyrin) 1, with a dibenzodiaza-30-crown-10 as a linker unit. Two structural features were examined. The aza-crown segment exhibited an intermolecular interaction with the zinc(ii) of the porphyrin, capable of causing aggregation to form spherical nanostructures, as inferred by concentration-dependency of (1)H NMR as well as scanning electron microscopy (SEM) observation. We also consider the crown-based conformation flexibility, in which accommodated K(+) tunes the porphyrin orientation into the tweezers conformation, assisting chirality induction upon complexation with chiral diamine 2. The circular dichroism (CD) intensity change essentially reached a plateau at a [(1R,2R)-2] : [1] ratio of 2 : 1 for which a 45% enhancement in the amplitude of CD spectra was observed compared to the K(+)-free conditions. Use of the crown linker of is not limited to promoting chirality induction with diamines in the presence of K(+); chiroptical probing of unprotected amino acids (Lys, His, Trp, and Phe) using 1 was attained through liquid (1 in CH(2)Cl(2))-liquid (the amino acids in 1 N KOH) two-phase extraction. The amphiphilic properties of the crown segment, as well as the K(+)-assisted tweezers conformation, make it possible to explore a potent way to develop chirality sensors for amino acids in water.     

配体形状对多吡啶铜(Ⅱ)配合物与DNA作用的影响

合成了一系列含有平面配体的Cu(Ⅱ)多吡啶配合物[Cu(IP)₂]²⁺、[Cu(PIP)₂]²⁺、[Cu(DPPZ)₂]²⁺和[Cu(HPIP)₂]²⁺，用吸收光谱、CD光谱和粘度等方法研究了这些配合物与小牛胸腺DNA的作用。结果表明配体上的取代基及配体的平面性对这些四面体配合物与DNA的结合强弱产生一定的影响。[Cu(DPPZ)₂]²⁺与DNA的结合较强，而[Cu(HPIP)₂]²⁺与DNA的结合较弱。CD光谱显示配合物[Cu(DPPZ)₂]²⁺、[Cu(PIP)₂]²⁺和[Cu(HPIP)₂]²⁺的加入会导致DNA的CD光谱减弱。而[Cu(IP)₂]²⁺的加入则会使DNA的CD光谱增强。同时，[Cu(IP)₂]²⁺与DNA结合后，还会引起一定程度的DNA构型转换，即DNA从B型转换成Z型。     

β-转角肽的溶液构象

主要报导TEM-1β-内酰胺酶的天然蛋白类抑制剂BLIP中一段多肽B1的溶液构象研究 结果.在磷酸盐缓冲溶液中,通过圆二色光谱、傅立叶红外光谱和核磁共振谱研究了B1的二 级结构特征.实验结果表明,B1在溶液中形成了β-转角结构,为在溶液中单独研究β-转 角结构形成与稳定性提供了良好的模板.β-转角在溶液中可以独立存在,表明β-转角在 蛋白质折叠过程中可能具有重要作用.     

Correlation of surfactant/polymer phase behavior with adsorption on target surfaces

In this contribution, the phase behavior of a surfactant/polymer mixed system is related to the adsorption of a complex derived from the mixture onto a target surface. The phase map for the system sodium dodecyl sulfate (SDS, a model anionic surfactant)/pDMDAAC (poly(dimethyl diallyl ammonium chloride), a cationic polymer) shows behavior very typical of surfactant/oppositely charged polyelectrolyte mixtures. The predominant feature is a broad, two-phase region in the phase map which lies asymmetrically around the 1:1 stoichiometry of surfactant charge groups to polymer charge units. The overall controlling principle driving the phase separation is charge compensation. Excess of polymer yields an isotropic solution, as does a great excess of surfactant (termed resolubilization). The phase separating in the SDS/pDMDAAC system is characterized by a positive zeta-potential when the polymer is in excess and a negative zeta-potential when the surfactant is in excess. The surface charge properties of the precipitated phases are essentially identical to those of target particles (ground borosilicate glass) dispersed at the same approximate position in the phase map, suggesting that the surfactant/polymer complex at the precipitation boundary is the same as that adsorbing onto the pigment particle. This conclusion is confirmed by depletion studies which allow the polymer adsorption density to be determined. For polymer-rich systems, essentially all of the surfactant adsorbs along with the polymer via a high-affinity isotherm with a plateau coverage of about 0.8 mg polymer/m (2). Surfactant-rich systems adsorb with a similar affinity, despite the mismatch of the complex charge matching that of the particle surface. Once adsorbed, these complexes are not readily removed by rinsing, though complexes adsorbed from SDS-rich systems will lose excess surfactant upon extreme dilution. Over a wide range of surfactant-rich compositions, from 1:1 stoichiometry out toward the resolubilization zone, a chemical analysis reveals that the surfactant/polymer precipitate species consists of a 1:1 charge complex with the addition of about 0.25 mol of surfactant/mol of complex. Resolubilization of these sparingly soluble species is achieved simply by dilution to below their solubility limit.     

聚赖氨酸为主链的牙刷状分子刷的可控合成

设计合成了溴基功能化的赖氨酸单体(Br-lys)并通过关环反应制备了对应的溴代L-赖氨酸N-羧酸酐(Br-Lys-NCA)单体.利用过渡金属引发剂Ni(COD)depe调控的NCA活性开环聚合和顺序添加单体的方法,得到了组成和结构明确的聚(ε苄氧羰基L-赖氨酸)-b-PBrLL(PZLL-PBrLL)两嵌段共聚肽.利用PZLL-b-PBrLL两嵌段共聚肽为大分子引发剂,通过ATRP引发甲基丙烯酸寡聚乙二醇酯(EGMA),合成了以聚赖氨酸为骨架的牙刷状分子刷.研究发现PZLL-PBrLL两嵌段在四氢呋喃中形成α-螺旋结构,螺旋度随着PBrLL链段的增长而降低,而PZLL-b-(PBrLL-g-PEGMA)形成部分α-螺旋构象,螺旋度随侧链PEGMA增长而减小.     

Chiral separation of dansyl-DL-amino acids with micellar systems containing copper (II) ion and N-n-dodecyl-L-proline in electrokinetic capillary chromatography.

Enantiomers of dansylated DL-amino acids were resolved by chiral copper (II)-N-n-dodecyl-L-proline (1) complexes incorporated in micelles of sodium dodecyl sulfate (SDS) in electrokinetic capillary chromatography (EKC). This resolution is caused by formation of diastereomeric ternary complexes consisting of chiral ligand 1, central copper (II) ion and enantiomeric amino acid derivatives in micellar phase. However, the resolution was not observed when SDS with an anionic polar head grop was replaced with dodecyl trimethylammonium brode (DTMAB) with a cationic polar head group. The ratio between copper (II) ion and 1 in the complex in either SDS or DTMAB was measured by UV-visible spectra, which respond to the d-d transition of copper (II). Mechanism of separation should be discussed in terms of effect of surfactant structures on constitution of copper (II) ion and 1 in the micellar phase and that of arene substituent structures linked to sulfonamide units in amino acid derivatives to be separated.