Tải bản đầy đủ - 0 (trang)
3 Interaction of Plasma Proteins with Water, Sugars and Nanosilica

3 Interaction of Plasma Proteins with Water, Sugars and Nanosilica

Tải bản đầy đủ - 0trang

25



Supramolecular Structures with Blood Plasma Proteins, Sugars and Nanosilica



307



1



268 K

2

263 K

253 K

243 K

3

233 K

7



(a)



6



5



4

3

δ (ppm)



2



1



0



10



(b)



8



6



4

δ (ppm)



2



0



–2



Fig. 25.1 1 H NMR spectra of unfrozen water: (a) BSA/water at CBSA = 2 wt% recorded at different temperatures and (b) HSA/saccharose/water at CHSA = 1 wt% and saccharose concentration

CSc = 0 (1), 0.1 (2) and 1 wt% (3) recorded at 250 K



several forms of water characterised by fast or slow (in NMR timescale) molecular exchange. The structural differentiation of water bound by proteins can occur

due to its interactions with hydrophobic and hydrophilic protein functionalities

[23, 24]. The water characteristics depend on the average number of the hydrogen bonds per molecule (nH ) [9, 24]. A decrease in the nH value is accompanied

by the displacement of the 1 H NMR signal towards the strong magnetic fields.

Consequently, the signals at smaller δ H values correspond to more strongly clustered (or more weakly associated) water characterised by a smaller number of the

hydrogen bonds per molecule.

There is a regularity of the albumin/sugar/water system corresponding to a sugar

concentration range giving a decrease in unfrozen water content. This is clearly

observed for the HSA solution with saccharose (Fig. 25.1b) since addition of 1 wt%

of saccharose leads to a decrease in the signal intensity of unfrozen water (at 250 K)

more than five times. The obtained results testify about effective interaction of sugar

with the protein molecules; i.e. the saccharose molecules can displace the major

portion of water bound to protein [25].

Addition of very small quantities of sugars leads to a decrease in the amounts

of unfrozen water. For fructose (Fig. 25.2a) this effect is in a narrow concentration

range. For glucose (Fig. 25.2b) a considerable decrease in the Cuw value is observed

only at CGl < 0.38 wt% and T near 273 K, and a section of an increase in Cuw

versus CGl is over a wide range of concentrations and temperatures. The greatest

changes in the amounts of unfrozen water are observed for the saccharose solution (Fig. 25.2c), and diminution in Cuw is greater at lower temperatures. At 250 K



308



V.V. Turov et al.

20000



273 K

263 K

258 K

253 K

243 K

233 K

223 K

213 K



12000



8000



20000



Cuw (mg/g)



Cuw (mg/g)



16000



273 K

268 K

263 K

253 K

243 K

233 K

223 K



25000



15000



10000



4000

5000

0



0

0.0



(a)



0.2



0.4



0.6



0.8



1.0



0.0



CGl (wt %)



10000



Cuw (mg/g)



0.2



(b)



0.4



0.6



0.8



CFr (wt %)



270 K

260 K

250 K



5000



0.0



(c)



0.5



1.0



1.5



CSac (wt%)



Fig. 25.2 Dependence of Cuw on concentration of sugars in aqueous solutions at different

temperatures: (a) fructose, (b) glucose and (c) saccharose



the signal of unfrozen water is not observed with increasing saccharose concentration CSac > 1 wt%. Thus, the aqueous solutions of glucose, fructose and saccharose

are characterised by different Cuw dependences on temperature and sugar content.

Therefore, one can assume that the effects of these sugars on the aqueous solutions

of proteins could be strongly different.

The interfacial energy γ S diminishes with increasing concentration of BSA in

the aqueous solution (Fig. 25.3a). Notice that similar dependences were observed

for other heterogeneous systems [9, 24]. Protein molecules are strongly hydrated;

therefore, to provide tight contacts between them (on self-association), a certain

quantity of bound water should be removed from intermolecular gaps to the bulk

that results in a decrease in the integral γ S value. Thus, the amounts of bound water

decrease as well as the γ S value with increasing protein content in the solution. The

difference in the γ S values determines the energy of self-association of the protein

molecules. Extrapolating γ S (CBSA ) dependence to the zero concentration gives the

interfacial energy of non-associated BSA molecules at γ S ≈ 450 J/g. The mentioned

effects can change on addition of sugars to the aqueous solutions of proteins.



Supramolecular Structures with Blood Plasma Proteins, Sugars and Nanosilica

500



500



400



400



300



300



γs (J/g)



γS (J/g)



25



200



2



1



200



100



100



0



0

0.0



(a)



309



0.6



1.2



1.8



CBSA (wt %)



2.4



0.0



3.0



(b)



0.2



0.4



0.6



0.8



1.0



CSug (wt %)



Fig. 25.3 Dependence of interfacial free energy on concentrations of (a) BSA in the aqueous

solution and (b) glucose at CBSA = 2 wt% (curve 1) or fructose at CBSA = 1.5 wt% (2) in the

ternary systems BSA/monosugar/water



The γ S (CSug ) dependences (Fig. 25.3b) have the shapes similar to the

Cuw (CGl(Fr) ) graphs (Fig. 25.2). Simple estimations show that in the 2 wt% BSA

solution 8.8 × 105 H2 O are present per protein molecule and ∼104 H2 O from them

are bound to macromolecules. Each sugar molecule can reduce a quantity of bound

water by ∼103 H2 O or even more since significant changes in the γ S value are

observed at CSug < 0.1 wt% (Fig. 25.3b). It is not possible to explain the substantial dehydration of BSA by only replacement of bound water by sugar molecules.

Therefore, one can assume that on the bonding of sugars to the protein molecules,

certain changes occur in the conformation of macromolecules that result in strong

diminution of the quantity of bound water. The effect of the significant dehydration of protein molecules in the presence of sugars (maximal at low temperatures)

can be one of the factors responsible for the cryoprotective properties of saccharides. Relatively small molecules of sugars (Fig. 25.4) can penetrate through cell

membranes, cause certain dehydration of intracellular structures and reduce the



Fig. 25.4 Silica A-300 nanoparticle (8.5 nm) and HSA (8 × 9.2 nm) and sugar molecules



310



V.V. Turov et al.

200



150



2.0



6



1



1.2



100



2



Interaction BSA-SiO2



Water

adsorption



1.6



γS(J/g)



–ΔG (kJ/mol)



2.4



BSA

solution



2.8



50



0.8



4



0.4



5



3

0



0



400



800



(a)



1200 1600 2000 2400



Cuw (mg/g)



0



20



40



60



80



100



Cuw (mg/g)



(b)



Fig. 25.5 Relationships between changes in the Gibbs free energy and the amounts of unfrozen

water for (a) BSA differently hydrated at CH2O = 95.8 (curve 1), 90 (2), 52.8 (3), 26.4 (4) and

13.2 wt% (5) for protein alone and on addition of 1 wt% of silica A-175 at CH2O = 89 wt% (6)

and (b) interfacial energy as a function of Cuw



formation of intracellular ice crystallites. Additionally, sugars do not have a negative influence on living cells because they can be easily utilised in the cellular

metabolism processes.

The relationships between the amounts of unfrozen water and its energetic characteristics for the solutions with BSA alone (Fig. 25.5a, curves 1–5) and on addition

of nanosilica (curve 6) suggest that practically entire amounts of unfrozen water correspond to SBW. A section corresponding to WBW is observed only for the 0.25%

BSA solution (Table 25.1).

The γ S values for the hydrated powder and aqueous solution of BSA are characterised by almost linear increase with increasing Cuw value (Fig. 25.5b) dependent

on protein hydration (total content of water CH2O ) (Fig. 25.2). For wet BSA powders, the maximum changes in the γ S value caused by the water bonding are equal



Table 25.1 Characteristics of bound water in hydrated BSA

No



CBSA

(wt%)



γS

(J/g)



s

Cuw

(mg/g)



w

Cuw

(mg/g)



– Gs

(kJ/mol)



– Gw

(kJ/mol)



1

2

3

4

5

6



0.25

10

47.2

73.6

86.8

10 (+1 wt% A-175)



193

76

52

29

11

65



1500

620

528

264

132

700



1700













3.4

2.8

2.8

2.8

3.0

2.8



1.6













s , SBW frozen at T < 250 K and G < −0.5 kJ/mol) and

Note. Types of water: strongly (Cuw

s

w

weakly (Cuw , WBW frozen at T > 250 K and Gw > −0.5 kJ/mol) bound waters.



25



Supramolecular Structures with Blood Plasma Proteins, Sugars and Nanosilica



311



to 70 J/g (Fig. 25.5b). Addition of 1 wt% of nanosilica to the 10 wt% BSA solution leads to changes in the γ S value decreased by 11 J/g. This value characterises

the interaction of silica nanoparticles with BSA causing the displacement of interfacial water bound to both macromolecules and nanoparticles. Notice that silica

(A-300) nanoparticles and albumin molecules (BSA and HSA molecules have close

sizes) have close sizes (Fig. 25.4) and the Am value (∼500 mg/g [24]) corresponds

to the protein monolayer adsorption at protein:silica ≈ 1:1, since their densities

twice differ. Therefore on the adsorption of albumins, macromolecules and silica

nanoparticles form hybrid aggregates characterised by certain changes in the protein

conformation affecting the adsorption of sugars.

An important task in immunology is the development of new methods of immune

activation using artificial antigens or vaccines, control of concentration and activity of antigens (antibodies such as immunoglobulin, Ig) [26]. Ig like other proteins

can irreversibly adsorb on silica [27]. The characteristics of Ig were described in

detail elsewhere [26, 28]. The Ig molecules (∼160 kDa, length ∼23 nm and average

diameter ∼5 nm) have a complex shape with two larger and two smaller polypeptide

chains bonding by disulphide bridges. Ig adsorption (A) versus pH has a bell-shaped

form at a maximum close to the PZC (or isoelectric point, IEP) of Ig at pH 6.6

(Fig. 25.6a). A similar A(pH) shape is typical for proteins as ionogenic macromolecules [24, 27, 29] because an area occupied by a molecule is minimal at the

PZC when it has the most compact shape and the repulsive electrostatic interactions

between adsorbed macromolecules are minimal. The appearance of negative charges

on the molecules at pH > pHPZC leads to a decrease in the adsorption (in comparison

with the adsorption at pH < pHPZC ) as a result of the electrostatic repulsion between

them and negatively charged silica surface. At pH < pHPZC adsorption decrease is

lesser because the electrostatic repulsion remains only between macromolecules but

not between the molecules and silica having pHPZC ≈ 3.5 and low negative surface

charge density at pHPZC < pH < 7 [24].

The Ig adsorption isotherms (Fig. 25.6b) have the Langmuir shape and the corresponding monolayer adsorption capacity is Am = 105 and 120 mg/g at pH 2.2

and 6.4, respectively. These Am values correspond to a minimal thickness of the

Ig adsorption layer due to its planar adsorption. Notice that for globular albumins

Am = 300–600 mg/g [24]. For proteins the adsorption and desorption isotherms do

not coincide because of difficulties of macromolecule desorption requiring simultaneous breakage of all intermolecular bonds between macromolecules and a solid

surface. Therefore, if desorption and adsorption (A ≤ Am ) of Ig occurs at the same

pH then the adsorption is practically irreversible. Desorption of Ig increases with

increasing amount of adsorbed Ig but the quantity of desorbed protein is small

(Fig. 25.6c) even at significant changes in pH.

The dependence of interfacial energy as a function of concentrations of Ig and

silica (Fig. 25.7) includes three specific sectors. At CSiO2 = 0, γ S (CIg ) represents

the modulus of the total changes in the Gibbs free energy of bound water changing

due to self-association of macromolecules. At CIg = 0 the γ S (CSiO2 ) dependence

describes the corresponding changes caused by interparticle interactions. If concentrations of both Ig and silica are not zero then the γ S (CIg ,CSiO2 ) dependence



312



V.V. Turov et al.

100



2



Ig Adsorption (mg/g)



Ig Adsorption (mg/g)



140

80

60

40

20



1



100

80

60

40

20

0



0

2



(a)



120



4



6



8



0.0



10



pH



0.2



0.4



0.6



0.8



1.0



Ceg (mg/ml)



(b)



Ig Desorption (μg/100 ml)



25

20

15

10

5

0

20



(c)



40



60



80



100



120



Ig Adsorption (mg/g)



Fig. 25.6 Adsorption of Ig on silica A-300 as a function of (a) pH (CIg = 0.075 wt%), (b) CIg

(pH 2.2 (1) and 6.4 (2)) and (c) desorption of Ig as a function of adsorbed amounts



is determined by both adsorption and coagulation processes. Taking into account

the Langmuir shape of the Ig adsorption at A < Am , one can assume that strong

coagulation of macromolecules interacting with different silica particles does not

occur at used concentrations. The Ig molecules are surrounded by a thick layer

of bound water (Table 25.2) whose thickness increases in dilute solutions with

decreasing concentration of proteins because in the dilute buffered solutions the

probability of formation of protein oligomers is low and undistorted hydrate shells

of macromolecules have a large thickness.

Maximum diluted Ig solutions (Table 25.2) are characterised by minimal Gibbs

free energy of bound water (the γ S value is maximal ∼400 J/g and Cuw ≈ 10 g/g at

CIg → 0) (Fig. 25.7). A small change in the interfacial energy at CIg = 3−10 wt%

can be explained by increased interaction between macromolecules leading to a



25



Supramolecular Structures with Blood Plasma Proteins, Sugars and Nanosilica



313



400

350

300

γS (J/g)



250

200

150

100

50



2



C SiO (



wt%)



0

2

4

6

8

10



0



2



4



6



8



10



CIg (wt%)



Fig. 25.7 Interfacial energy as a function of concentrations of Ig and silica A-300



Table 25.2 Characteristics of water bound in hydrated Ig and suspensions of A-300 and Ig/A-300

CIg / CSiO2

(wt%)



Csolid .

(wt%)



γS

(J/g)



s

Cuw

(g/g)



w

Cuw

(g/g)



– Gs

(kJ/mol)



– Gw

(kJ/mol)



1/0

1.65/0

3.3/0

5/0

6.5/0

10/0

0/4.7

0/7

0/9

2.2/3.3

1/3.3

2.7/2.5

1.2/2.5

4.9/0.25

5.3/0.5



1

1.65

3.3

5

6.5

10

4.7

7

9

5.7

4.3

5.2

4.7

5.05

5.8



352

280

187

203

197

205

106

59

27

162

149

115

200

45

107



2.1

2.1

1.7

2.0

2.2

1.7

0.7

0.6

0.25

1.8

1.1

0.8

0.8

0.5

0.75



9.9

7.9

3.8

5.0

4.8

5.3

2.5

1.6

1.0

6.2

6.9

5.2

6.2

2.5

4.25



3

2.5

2.4

2.5

2.7

2.9

2.4

2.6

2.2

3

3

4

4.8

3

2.2



0.7

0.5

0.7

0.7

0.5

0.5

1

0.5

0.6

0.5

0.5

0.4

0.3

0.25

0.3



decrease in the amounts of bound water per macromolecule. Interactions between

macromolecules and silica nanoparticles are much stronger than between macromolecules; therefore, silica added to the Ig solution leads to diminution of the

amounts of water bound by protein. The reduction of the γ S value for the system Ig/A-300/water is maximal at small CIg values because relative adsorption is



314



V.V. Turov et al.



maximal at minimal CIg values (e.g. with increasing CIg,eq from 0.1 to 1.0 mg/ml

the adsorption increases only twice (Fig. 25.6b)). At CIg > CSiO2 changes in the

γ S values are relatively small due to weak interaction of Ig monolayer coated

silica nanoparticles with dissolved protein molecules. This is confirmed by the

rheometry results showing an extremal dependence of the viscosity of the protein

(polymer)–nanosilica suspensions on concentration of proteins (polymers) [24].

For treatment of certain diseases (e.g. wound and purulent infections of internal cavities), preparations based on nanosilica are successfully used [5]. In some

of these cases silica nanoparticles can contact blood. Blood as a multicomponent

heterogeneous system contains many types of cells and macromolecules, and the

aqueous solution of low molecular organic and inorganic compounds plays a role of

the dispersion medium. Therefore investigations of hydrate shells of blood components, intermolecular interactions between them alone and on contact with solid

nanoparticles are of importance for deeper understanding of the mechanisms of

actions of medicinal nanocomposites.

Fibrinogen is one of the main plasma proteins participating in blood clotting

[30, 31]. Its concentration in blood is 0.22–0.44 wt%. Native HPF molecules

(340 kDa, 46 × 6.5 nm) are strongly hydrated, and bound water can play an important role in HPF interaction with other components of blood or solid nanoparticles.

HPF molecule is composed of two identical molecular halves consisting of three

non-identical Aα-, Bβ- and γ-chain subunits (compared in size with primary silica

nanoparticles) held together by multiple disulphide bonds; or according to another

model, a HPF molecule includes one central nodule (E domain) and two identical

outer nodules (D domains) linked by two coiled-coil regions. HPF molecules have

“loose ends” which are extremely mobile that can be functionally important, and

they can play a specific role on the adsorption of HPF especially onto non-planar surfaces as of nanosilica. AFM investigations of adsorption of HPF on a silica surface

showed that it is predominantly adsorbed through D and E domains [32].

The adsorption isotherm of HPF at pH 7.4 and Ceq < 0.3 mg/ml (Fig. 25.8a)

has the Langmuir isotherm shape and Am = 156 mg/g for planar-adsorbed long

molecules at Ceq ≈ 0.25 mg/ml, since for vertically adsorbed molecules Am ≈

500 mg/g at Ceq ≈ 0.5 mg/ml (Fig. 25.8a). A maximum of A(pH) is at pH 5.5–6.0

(Fig. 25.8b) close to the PZC of HPF. The adsorption decreases with increasing

pH like other plasma proteins [24, 33]. Desorption of HPF is low [34] as for Ig

shown above that suggests irreversible planar adsorption of HPF. The right term of

the Langmuir equation was used as the kernel of integral adsorption equation [24,

34] to calculate the distribution function of Gibbs free energy of adsorption f( G)

(Fig. 25.8c). The position of the f( G) maximum at – G ≈ 2.2 kJ/mol corresponds

to the slow rise of the adsorption isotherm and is in agreement with the Gs values

calculated from the 1 H NMR data for SBW (Table 25.3). These not-large values

– G < 5 kJ/mol (Fig. 25.8c) are due to a considerable diminution of the solvation

energy of HPF on adsorption to the silica surface.

The maximum concentration of water bound by HPF (or A-300 alone) and maximal γ S values are observed in more diluted solutions (Table 25.3 and Fig. 25.9) like



25



Supramolecular Structures with Blood Plasma Proteins, Sugars and Nanosilica



315



Fig. 25.8 HPF adsorption as a function of (a) equilibrium CHPF (PBS, pH 7.4); (b) pH (CHPF =

0.0795 wt%); and (c) distribution of Gibbs free energy of HPF adsorption at A < 160 mg/g

Table 25.3 Characteristics of weakly (WBW) and strongly (SBW) bound waters in solution of

0.15 M NaCl, HPF in PBS, suspensions of A-300 and HPF/A-300

Sample

NaCl

A-300a

A-300b

A-300b

HPFc

HPFc

HPF/

A-300c

HPF/

A-300c

HPF/

A-300c

HPF/

A-300c



CHPF

(wt%)



CSiO2

(wt%)



s

Cuw

(g/g)



w

Cuw

(g/g)



– Gs

Smes

(kJ/mol) (m2 /g)



Smac

(m2 /g)



Vmes

Vmac

(cm3 /g) (cm3 /g)



1.25

2.5

1.6

1.0

8.0

6.75

3.65



2.2

2.4

2.6

2.2

2.2

3.0

2.6



315

115

160

169

819

545

71



24

64

26

2

506

185

145



1.15

1.20

1.54

1.19

2.22

3.02

0.16



0.59

2.00

0.66

0.06

11.78

4.96

3.84



1.25

2.5

0.6



2.5



0.5

0.7

0.6

0.25

6.0

1.25

0.35



2.5



1.7



1.25



1.75



3.0



323



43



2.31



0.69



2.5



3.5



0.6



3.1



3.0



57



137



0.21



3.49



2.5



5.2



0.4



0.4



4.5



112



6



0.70



0.10



4.7

7.0

9.0



a Aqueous

b 0.15



suspension without addition of NaCl.

mol NaCl.



c PBS.



Ig and BSA. For instance, at CHPF = 1.25 wt%, HPF hydration corresponds to Cuw

= 14 g of bound water per gram of protein, but Cuw = 8 g/g at CHPF = 2.5 wt%;

i.e. twice larger CHPF value gives twice smaller Cuw value. A similar effect was



316



V.V. Turov et al.



600

500

400



ΔγS of HPF coagulation



γS (kJ/mol)



ΔγS of HPF self-association



ΔγS of particle-particle interaction



700



300

200

100

00

C

Si

O

2



2



4



(w



t%



)



6



8

10



0.0



0.5



1.0



2.0

1.5

CHPF (wt%)



2.5



3.0



Fig. 25.9 Interfacial energy γ S as a function of concentrations of HPF and silica



explained above for BSA and Ig as enhanced protein–protein interaction leading to

the displacement of a fraction of bound water to the bulk. For HPF/A-300/water,

a sharp decrease in the interfacial energy (in comparison with HPF alone) is characteristic similar to other proteins. In the HPF/A-300/water systems a decrease in

concentrations of both SBW and WBW is observed (Table 25.3), and interpretation

of this effect is the same as for Ig discussed above.

The surface forces (adhesive forces) at the interfaces of HPF/water can be estimated if the specific surface area of protein molecules is known. From the shape

of HPF molecules [32] assuming a simplified geometry for them (two spheroids of

6.5 nm in diameter, a spheroid of 5 nm in diameter, cylindrical section of 1.5 nm in

diameter and 29.5 nm in length) it is possible to calculate the surface of a molecule

equal to 360 nm2 . This gives the specific surface area of protein S = 750 m2 /g (close

to Smes + Smac for the 2.5 wt% HPF solution, Table 25.3). G as differential Gibbs

free energy is numerically equal to differential energy of adhesion:

G = −Wa .



(25.1)



The interfacial energy γ S is equal to the total energy of adhesion, and the

adhesive forces can be estimated as [35]

F=



G/x,



(25.2)



where x is the thickness of a bound water layer (estimated from the geometry of HPF

molecule and the Cuw value). The range of adhesive forces increases up to 3 nm

with decreasing concentration of HPF (Fig. 25.10) that is caused by a decrease in

polymer–polymer interactions in the more diluted solution.



Supramolecular Structures with Blood Plasma Proteins, Sugars and Nanosilica



Fig. 25.10 Radial

dependence of adhesive

forces in the aqueous solution

of HPF at CHPF = 1.25

(curve 1) and 2.5 wt% (2)



317



250

200



F (GN/g)



25



150



1



100



2



50

0

0.0



0.5



1.0



1.5



2.0



2.5



x (nm)



Water or other liquids can be frozen in narrower pores at lower temperatures as

described by the Gibbs–Thomson relation for the freezing point depression

Tm = Tm (R) − Tm,∞ =



2σsl Tm,∞

k

=− ,

Hf ρR

R



(25.3)



where Tm (R) is the melting temperature of a frozen liquid in pores of radius R, Tm

the bulk melting temperature, ρ the density of the solid, σ sl the energy of solid–

liquid interaction, Hf the bulk enthalpy of fusion and k a constant. This equation

(or related integral equation) was used to calculate the size distribution functions

of pores f(R) (cavities, voids) filled by unfrozen water in frozen aqueous solutions of macromolecules, suspensions of nanosilica, etc. [9, 24, 36]. For the HPF

solutions, these distributions are broad (Fig. 25.11b) as well as for the nanosilica

suspension (Fig. 25.11a). For the HPF/A-300/water, a considerable rearrangement

of hybrid aggregates occurs with increasing component concentration that reflects in

f(R) changes (Fig. 25.11c). These results reveal a significant decrease in the cavity

volume filled by unfrozen water due to displacement of significant amounts of this

water to the bulk because of strong macromolecular–particle interactions in hybrid

aggregates becoming more compacted with increasing HPF and silica content.

HPF fulfils an important role in blood clotting. On contact with air HPF reacts

with thrombin detaching a HPF fragment transforming it to active fibrin-monomer

(Fm). Fibrin can easily polymerise to form supramolecular fibrin-polymer (Fb).

Transformation of HPF into fibrin-polymer through the stage of fibrin-monomer

is accompanied by a significant change in the characteristics of bound water

(Fig. 25.12), and a decrease in both SBW and WBW is observed. These changes

reflect in the γ S dependence on composition of the system since it decreases from

600 J/g for non-associated HPF molecules and 160 J/g for Fm to 10–20 J/g for Fb.



Tài liệu bạn tìm kiếm đã sẵn sàng tải về

3 Interaction of Plasma Proteins with Water, Sugars and Nanosilica

Tải bản đầy đủ ngay(0 tr)

×