Surface Chemistry

Lecture 8
Date 04/12/20
 Repulsive Interactions
Leading to total pair potential (attractive + repulsive)

• Repulsion is required to maintain molecular integrity

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 Repulsive Interactions
Leading to total pair potential (attractive + repulsive)

• Two types of repulsive interactions:

1. Columbic repulsion between two like charges
2. Repulsion between two uncharged particles brought too close to
each other
As electron cloud mixing is involved over short distances the repulsive
force increases exponentially with distance due to Pauli’s principle
which forbade electron of one molecules from entering into occupied
orbital of other molecule.
Hard core or Born repulsion
• Assumes each shell as hard core
• These are Q.M. repulsions
• No exact equation for calculation
• Responsible for fixed density of solids and liquids
 Repulsive Interactions
Van der Waals radius
• Distance beyond which repulsive forces are negligible
• After that req further decrease in r will exponentially increases
repulsive forces.

For atom as hard sphere req is obtained from

• For gases from PVT data, η, solubility, spectroscopic data

• For liquids self diffusion , compressibility measurements
• For solids X-ray diffraction and neutron diffraction techniques
 Repulsive pair potential
Van der Waals radius calculation
• For two hard sphere molecules repulsive pair potentials is
represented by an inverse power law of the type

• m=8 or 16 usually
• V =0 at r >rw
• V=>∞ 𝑎𝑡 r < rw

• Equilibrium separation is achieved when attraction⇆ repulsion

• Total intermolecular pair potential

Vt = V attraction + V repulsion
 Hydrogen Bonding Attraction

• H-bonding attraction is a donor accepter attraction involving H-

atoms
• They exists between electronegative atom and with H atom
covalently bound to a similar atom.

• Q.M. in nature
• Electrostatic in nature
 Hydrogen Bonding Attraction

• Previously it was labeled as quasi-covalent in nature

• Now it is believed to be electrostatic in nature.
• Acid base concept not 100% applicable
• There is no 100% proton transfer during this interaction
Covalent bond Ionic bond
If the electron are able to E.N. is power to attract
occupy resulting MO, the bond electron towards itself.
will have some covalent E.N difference partial ionic
character. character

H bond
When es of H is attracted by a more electronegative atom with which H is
covalently attached and H is left partially unshielded. Now neighboring atoms
exhibits e pair less tightly bound to its own nucleus. Further H proton effective +ive
field more concentrated over small volume. Generating electrostatic force. The
result is concentrated _ive and localized +ive charge in each molecule.
 Hydrogen Bonding Attraction
MOT description of H-bond
• First Is orbital of H and valance orbital of E.N. atom overlap to
from a BMO and an AMO.
• BMO accumulates what will act as lone pair for H-bond overlap
• The BMO, AMO of covalent bond gets overlap with N.BO of more
electronegative atom and generates new BMO, HBMO and AMO.

F H
 Hydrogen Bonding Attraction
MOT description of H-bond
Lowering of energy as a
result of overlap makes H
bond a stable interaction
ABO

ABO

HBMO
NBO
BMO NBO of
electronegative
part contributing
BMO molecule
BMO of H donating
molecule
F H------------------ F H
 Hydrogen Bonding Attraction
H-bond
• A sort of coordinate covalent bond
• A sort of electrostatic interaction
• A sort of Lewis acid base interaction
No interaction type is 100% satisfied
It has;
MO overlap character
Electrostatic + covalent character
Like Lewis acids es- receiving character

H bonding gives water;

• Stability C2H50H has high B.P. than
• High m.p and b.p. CH3OCH3 due to H bonding
• Latent heat of vaporization
• Universal solubility
• Very low compressibility
 Hydrogen Bonding Attraction
H-bond
H2O has strong H bond than methanol due to;
• Two H bond per molecule
• Availability of two strong +ive field per water molecule
• C2H5 as electron donating inductively will hinder effective MO
overlap.

H bonding as life coordinator

• All biological molecules maintain their specific geometry due to

=OH and –NH h bonding
• All proteins primary and secondary structure which is necessary fro
performing catalytic effects
• H2O aligns specifically around particular site due to H binding
• DNA Retains helical structure. DNA denatures in lethal diseases
such as cancer.
 Hydrogen Bonding Attraction
Properties of H bonding

1. Bond length 0.12-0.23

2. Strength 1-40kJ/mol
3. Weaker than covalent bond (=150kJ/mol)
4. Weakest H bond (<4kJ/mol) = vander waals intercation
5. Strong H-bond 14-40
6. Moderate H-bond 4-15
7. Directional
8. α1/T
9. Bond formation exo thermic
10. Bond breakage endo-thermic
Experimental detection:
IR, X-ray diffraction, NMR, Neutron diffraction, neutron inelastic
scattering method, computational methods with LCAO in DFT/Ab-
initio methods
 Hydrogen Bonding Attraction
Properties of H bonding

1. H2O stronger of all H bonding

2. Two H bonds per molecule yield 3d network

4 bonds per H2O molecule

O-H 0.100nm
O—H 0.176
, van der Waals radius revealing
overlap is there

Tetrahedral arrangement of 4 H
bonds per molecule generates
hexagonal pattern
 Hydrogen Bonding Attraction
Properties of H bonding

Tetrahedral arrangement of 4 H bonds

per molecule generates hexagonal
pattern

Fluidity does not

allow 4 bond to
be in place for
longer time.
Bonds formed
breaks and then
reform with other
neighbors
 Hydrogen Bonding Attraction
Properties of H bonding

In ice molecules are at fixed position

makes the structure with empty
spaces and density of ice gets lower
than that of water
Close packing
reduces density
but in ice density
is lower due to
loss of fluidity.

This is known as
association of
liquid water
 Hydrogen Bonding Attraction
Association of liquid water=> unusual properties
1. Density increases from 0-4ºC due
to breakage of large associates
leading to close packing of small
associates.
2. Dielectric constant increases as
liquid solidifies
3. Low compressibility of water than
ice is close packing of molecules
in water than in ice.
4. Unusual solubility as both solvent
and solute. It can dissolve ionic
compound as can form strong
solvate and shield opposite ions
Hydrophilic and hydrophobic interactions
Lyophilic and lyophobic interactions
1. Lyophillic= solvent loving
2. Lyophobic = solvent hating Small non polar solute
Hydrophobic interactions:
1. Non polar solutes break few H bonds leading to increase in
energy of system.
2. System will try to regain lowest energy state.
3. It will bring similar molecules together.
4. Forming larger aggregate
5. Until it separate out as separate phase
6. System re-attains H- bonding network.
7. If the concentration of non polar molecule is small and it
exhibit small size then it can fit in to the empty space of H
bonding network.
8. At Small concentration water will form a cage around solute called
clatherate. the caged molecule now cannot develop any outer interaction.
 Hydrophilic and hydrophobic interactions
Lyophilic and lyophobic interactions
1. If non polar size is larger the molecule does not fit in the normal
cavity. Organizing water molecule around larger solute makes
entropy unfavorable. Disrupting tetrahedral water molecules
leading to instability in the system.
Δ S = -ive and -TΔ S = +ve
Δ H = 0 as no solute solvent attraction developed
Δ G = Δ H + TΔ S = +ive = non spontaneous process,.
At high T:
Thermal motion breaks clatherate and Δ S = 0. water solute
disoriented and solute can move to form larger aggregate.
Similar attract each other. ΔH is positive and this is met by heat
supplied to the system in form of high T
For hydrophobic system;
Δ H = 0 at low T
Δ H = +ive at high T
 Hydrophobic interactions
1. Hydrophobic effect.
Hydrophobic effect separate the proteins from surrounding solvent
forming gobbler structure and then internal cavity H-bonding retains
their secondary structure.
2. Hydrophobic intercations are strong interactions between
hydrophobic molecules or surface in water. It is often more strong than
their attraction in free space. E.g. methane molecules interaction
energy is -14 x10-21 J in water which was -2.5 x10-21 in free space.
• Hydrophobic-hydrophobic is stronger than solute-solvent
interaction
• Strength of hydrophobic interaction >> strength of van der waals
interactions
• Surface area of HC determines magnitude of free energy transfer.
• ↑ Hydrophobicity in a molecule e.g. non polar character ↑
hydrophobic interactions
 Hydrophobic interactions applications

Basic of attachment of SAM formation,

particles in froth flotation structure
process, protein
conformations

micelle formation biological membrane

 Hydrophilic interactions
• Generally polar molecules
Hydrophilic functional groups;
• May be capable of H- bonding
• _COO-
• Strong affiliation with water • _SO3-
• True solvate formation • _SO4-
Examples; • OPO2-
High EN containing molecules • _[+NH(CH3)2]
Strong hydrated ions • _[+N (CH3)3]
• _[NO(CH3)]
Alcohols,
• _NH2
Glycerol's • _OH
Glycols • _POCH3
Glucose etc. • _SOCH3

Hydrophilic group prefers to get attach with water molecules rather

than with each other
 Hydrophilic interactions
• Hygroscopic (absorbs moisture from air)
Form hydration shell
Disorder water molecules to form own solvates
• This lead to protein unfolding
• Some hydrophilic groups when attached to hydrophobic groups e.g. HC
their hydrophilic activities get masked. E.g. _OH, _ OCH3, _ SH, _ NH(CH3)
_ CONH2, _ NO & _ NO2 , _ CHO.
The surfactants have a characteristic
molecular structure consisting of a
structural group that has little/no
attraction for solvent, known as
lyophobic group, together with a group
which has strong attraction for solvent,
called lyophillic group. Thus surfactants
have amphiphillic structure with a polar
head and non polar tail.
;

Properties

Adsorption
at the Orientation Micellization
interface
 Adsorption at the interface
Fig.1

Fig.1
Whenever dissolved in water or hydrophilic
Whenever dissolved in solvent, the presence
solvent,the presence of lyophobic group in the
solvent distort the solvent molecules, the
of lyophobic group in the solvent distort the
solvent pushes the surfactant towards the
surface in order for the system to attain the
solvent molecules, the solvent pushes the
lower free energy but lyophillic group prevents
the surfactant from being expelled completely
surfactant towards the surface in order for the
from the solvent as a separate phase. The
surfactant can also adsorb on the surface of
system to attain the lower free energy but
hydrophobic liquid but with opposite
lyophilic group prevents the surfactant from
orientation.

being expelled completely from the solvent as

a separate phase.
Adsorption at the interface
Orientation:
•The amphiphilic structure of surfactant
causes orientation of the molecule at
the surface with their lyophilic end in
the solvent and lyophobic end oriented
away from the solvent.

Fig 2. Orientation in A) polar solvent. B). nonpolar

solvent.