Seyed Mohammad Motevalli

Fall 2014

Size and coating of nanoparticles have effect on

their thermodynamic interaction with proteins

1

Shahid Beheshti University

IRAN

Outline:Corona

Hard

Soft

Nanoparticle features:

Size• SPR

• Shape

• Zeta potential

Coat• Type

• Charge

• Hydrophobicity

• Density

Protein features:

Molecular weight

Charge

Hydrophobicity

Structures

• Secondary

• Tertiary

Thermodynamically

interaction

Gibbs free energy

Equilibrium constant2

Corona

Hard

• Nanoparticle

fingerprint

• Less exchange rate

• More affinity

Soft

• Outer layer

• More exchange rate

• Less affinity

3

• W. Liu et al. 2013.

• M. P. Monopoli et al. 2010.

• I. Lynch et al. 2008.

Nanoparticle features:

Size• SPR

The collective oscillation of the

conductive electrons

• Shape

decrement of spherical shape is

usually with blue shift in UV-

absorbance diagram

• Zeta potential

The electric potential at the boundary

of the double layer

4

• V. Juve et al. 2013.

• M. De et al. 2008.

• A. Albanese et al. 2012.

• J. D. Clogston et al. 2011.

• Type

There are metallic and non-metallic NPs

• Charge

Different coatings have different charge (negative-neutral-positive)

• Hydrophobicity

Based on functional groups

• Density

Density of coating derivatives effect on protein adsorption

Nanoparticle features:

Coating

5

• Z. Wang et al. 2009.

• L. Ramajo et al. 2009.

• M. Lundqvist et al. 2008.

• V. Mohanraj et al. 2007.

• C. D. Walkey et al. 2011.

• Smaller amino acids

side chain have more

flexibility

• Heavier proteins have

more contact positions

Protein features:

Molecular weight

6

• R. Najmanovich et al. 2000.

• M. Lundqvist et al. 2008.

• Additional protein net

charge, the positional

net charge is important

too

• NP surfaces may take

up proteins depending

on their pI in a rather

narrow pH range

Protein features:

Charge

7

• K. H. R. Choo 2008.

• M. Mahmoudi et al. 2011.

• Globular proteins have lesser tend to smaller NPs

• Proteins with less than 200 residues usually have more

hydrophobicity

Protein features:

Hydrophobicity

8

• H. Liao et al. 2005.

• J. Klein. 2005.

• Z. Weng et al. 2001.

Secondary

• sheet structure have

more entropy

• Charge amino acids

usually are part of helix

structures

Tertiary

• Encounter position

• Conserved sequences

have more stability

Protein features:

Structure

9

• W. Yeh. 2005.

• H. Liao et al. 2005.

• H. S. Frank et al. 1945.

• Hydrophobic aminoacids usually havemore flexibility

• Smaller NPs havelesser contact positionsthan larger NPs

• Free change Gibbsenergy in larger NP-protein is more thansmaller ones

Thermodynamically interaction:

Gibbs free energy

∆𝐺 = ∆𝐻 − 𝑇∆𝑆

10

• G. D. Rose et al. 1985.

• M. Lundqvist et al. 2008.

• J. M. Hayes et al. 2012.

Thermodynamically interaction:

Gibbs free energy

11

• S. T. Yang et al. 2013.

Thermodynamically interaction:

Equilibrium constant

12

• F. D. Sahneh et al. 2013.

13

Contact orientation:

14