Interparticle interaction
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1 Colloid chemistry for pharmacists Interparticle interaction Levente Novák, István Bányai Dep. of Colloid- and Environmental Chemistry 2. lecture 1
2 Characterization of colloids colloidal state parameters 1. Dispersity (or size distribution) 2. Morphology (shape, inner structure) 3. Spatial distribution 4. Interparticle interaction 2
3 4. Molecular interactions The origin of interactions between colloidal particles: the interactions between individual molecules. Ion 1 - ion 2 (rare, macromolecules) Ion 1 - permanent dipole 2 (rare, mixtures) permanent dipole 1 - permanent dipole 2 permanent dipole 1 - Induced dipole 2 instantaneous dipole 1 - Induced dipole 2 Hydrogen-bonding interaction Repulsion Hydrophilic and Hydrophobic interaction 3
4 Molecular interactions Sign: attraction (-), repulsion (+) Coulomb: ion-ion ion-dipole dipole-dipole E E di 12 Coul Orientation effect ( ze) 1( ze) r ( ze) 2 1cos 1 4 r a) T low b) T high Acting range~50nm kj/mol Range~1.5nm 15 kj/mol r~ distance 4
5 Molecular interactions dipole-dipole (orientation effect) a) T low, the constant gives the sign: +2 parallel, -2 antiparallel oriientation E dd 1 2 konst r 0 At low temperature the orientation effect yields an ordering! 2 kj/mol b) T high, freely rotating dipoles, always attraction: 0.3 kj/mol 3 range~1.5nm E dd (4 ) kbt r 5
6 Molecular interactions dipole-induced dipole first dipole: electron fluctiation E id 1 2 ~ r 6 induced-induced dipole 6
7 London dispersion interactions E ti 12 I = ionization energy 3 II ~ I1 I2 (4 0 ) r Dispersion forces are weak, short-lived forces, which are experienced by all molecules. They operate over very short distances. saturated vapour pressure: CH 3 Cl <CH 2 Cl 2 < CHCl 3 <CCl 4 London forces depend on the shape; evaporation heat: pentane> isopentane> neopentane Range~0.4nm 2 kj/mol London dispersion interactions (London forces tend to increase with molecular weight, some properties of liquid are approximately proportional to the energy of intermolecular attraction: melting point, boiling point, vapor pressure, surface tension, viscosity) Additive! 7
8 Molecular interactions (bulk) Induction effect Dipole makes polarization Dipólmomentum molekula Debye molekula Debye molekula Debye HF 1.91 SO2 1.6 Metanol 1.7 HCl 1.05 CO 0.1 Etanol 1.7 HBr 0.79 CO2 0 Aceton 2.86 H 2 O 1.85 Fenol 1.45 H 2 S 0.93 NH D= Cm, Dipolmoment, in Debye unit α, polarizability,, polarizability, Polarizálhatóság He 0.2 CO 1.65 CH 2 =CH H H 2 O 1.44 C 2 H Ar 1.63 O C 6 H Xe 4 Cl NH CCl CH , m 0 The polarizability increases with volume (mass). 8
9 Sum of induction, orientation and dispersion to the same type of molecules: β Boer and Hamaker for macroscopic phases, particles: A: Hamaker constant, q: pieces atoms /volume, A ~ 2 q E r J A 6 ~ 11, Jm 6 CCl Etanol 3.4 Benzol 4.29 Cl-benzol 7.57 F-benzol 5.09 Toluol 5.16 víz 1.82 Compound /Debye orientation induction dispersion CCl Ethanol Benzene Water % 9
10 Attraction- repulsion (total interaction) between molecules (Lennard-Jones (6:12) potential repulsion E tot konst. 11 ~, 12 6 r r J attraction 10
11 Hydrogen-bonding interaction H-bonding interactions a donor acceptor interaction involving H atoms. They exist between electronegative atoms such as O, N, F, with H atoms covalently bound to similar electronegative atoms. Hydrophobic interaction Hydrophobic interaction describes the strong interaction between hydrophobic molecules or surfaces in water. This is often stronger than their attraction in free space. Hydrophilic molecules are mostly polar and have a H-bonding capacity Why are non-polar molecules hydrophobic? Non-polar molecules share a common characteristic: practically no intermolecular forces can form between them and water (only dispersion forces). For a molecule to be watersoluble it must be able to experience dipolar interactions, or form hydrogen bonds, with water. 11
12 Hydrophobic, hydrophilic interaction Hydrophobic and hydrophilic interactions: Some molecules such as hydrocarbons, oil, fats, inert atoms, fluorocarbons and some polymers that are incapable of forming H-bonds and do not like to interact with water, are called hydrophobic molecules. Hydrophobic means water-fearing or waterrepelling. The more general name lyophobic, which means solvent repelling. Hydrophilic molecules are mostly polar and have a high H-bonding capacity. In practice, hydrophobic molecules, in contact with water, prefer to interact with each other instead of the water and try to minimize their total surface area and form a water immiscible phase. Hydrophobic interaction describes the strong interaction between hydrophobic molecules or surfaces in water. The interaction between a hydrophobic molecule and water is actually attractive, due to dispersion interactions. However, the interactions between water is much more attractive due to H-bonding interactions, so water has the effect of squeezing the hydrophobic molecules to attract each other to form a larger aggregate, reducing the total free energy of the system. 12
13 Examples 13
14 Molecules of a watersoluble compound and molecules of water mix freely with each other: the two types of molecules are able to mix completely. If a compound is insoluble in water, its molecules cannot mix freely with molecules of water.: instead, the two types of molecule remain completely separate. Occasionally, a small amount of the solute dissolves, while the majority floats on top of the solution. 14
15 ion-dipole The hydration of ions by water molecules. The interaction of ions by water molecules, is a dipolar interaction, which exists between the charge of the ion and the partial charge on the polar water molecule. Colloids: hydration of proteins 15
16 The alcohols are polar molecules. Electrons are withdrawn towards the highly electronegative oxygen atom, distorting the distribution of electrons throughout the molecule as a whole. Consequently, the molecule is polar. Examples: H-bond Molecules of an alcohol can form hydrogen bonds with water, and with each other. *Crowe, J.:Chemistry for the Biosciences Oxford UP. ISBN ,
17 Examples Glycerolphospholipids arrange themselves in two sheets, each with a hydrophilic and a hydrophobic face. The hydrophobic faces of the two sheets lie against one another, forming a sealed, water-free layer. *Crowe, J.:Chemistry for the Biosciences Oxford UP. ISBN ,
18 examples The folding of a polypeptide possessing hydrophobic and hydrophilic portions. The darker hydrophobic portions fold away from the aqueous surroundings; this arrangement is stabilized by dispersion forces which operate between the tightly packed hydrophobic portions. *Crowe, J.:Chemistry for the Biosciences Oxford UP. ISBN ,
19 Examples The sequence of monomers within a polymer. Side chains that are in close proximity when a polypeptide chain adopts its three-dimensional, folded structure may be some distance apart in the polypeptide chain itself. Look at this polypeptide chain, and notice how amino acids A and B are some distance apart in the sequence of the polypeptide chain, but actually come into close proximity when the chain is folded *Crowe, J.:Chemistry for the Biosciences Oxford UP. ISBN ,
20 Summary The various noncovalent forces that can operate in a biological molecule, such as a polypeptide *Crowe, J.:Chemistry for the Biosciences Oxford UP. ISBN ,
21 The interrelationship between primary and secondary structure. The ability of a biological polymer to fold into regions of characteristic secondary structure depends upon it possessing an appropriate primary structure. Secondary structure is stabilized by hydrogen bonds. The shape of larger molecules: structure of proteins: 1 chemical + 3 colloidal 21
22 Structure of proteins: 1 chemical + 3 colloidal The regular positioning of hydrophobic amino acid residues in the primary sequence of a- keratin generates a hydrophobic patch around one face of the a-helix when the polypeptide adopts is folded, threedimensional structure. Adapted from C.Dobson et.al. Tertiary structure (3 dimensional shape) An keratin molecule possesses numerous - helices, which lie adjacent to one another when the molecule packs into its native three-dimensional conformation: its tertiary structure. Crowe, J.:Chemistry for the Biosciences Oxford UP. ISBN ,
23 Structure The protein hemoglobin comprises four polypeptide subunits, and depend upon both intramolecular and intermolecular forces to ensure that its structure remains correct. Hemoglobin comprises four molecules, which are held together by intermolecular forces 23
24 Effect of bulk environment 24
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