The document discusses how the size and coating of nanoparticles can affect their thermodynamic interaction with proteins. It outlines that nanoparticle features like size, shape, zeta potential, and coating type/charge/hydrophobicity can impact protein adsorption. Protein properties such as molecular weight, charge, hydrophobicity, and secondary/tertiary structures also influence the thermodynamic interaction. The Gibbs free energy and equilibrium constant of the nanoparticle-protein interaction depend on these factors.
Nano technology in textiles. seminar. pptxBademaw Abate
The application of nanotechnology in textiles is growing so fast. The main difference b/n nano finishing and conventional finishing is durability, comfort and breath-ability enhancement in nano finishes.
Introduction
History
Definition
Types of H bond
Hydrogen bond in water
Bifurcated and over - Coordinated hydrogen bond in water
Hydrogen bonds in DNA and proteins
Hydrogen bonds in polymers
Systematic hydrogen bond
Importance of hydrogen bond
Conclusion
References
Conducting polymers are those polymers which conduct electricity due to extended P- orbital system. Due to this extension of P orbital electrons can move from one end to another end of the polymer.
Nano technology in textiles. seminar. pptxBademaw Abate
The application of nanotechnology in textiles is growing so fast. The main difference b/n nano finishing and conventional finishing is durability, comfort and breath-ability enhancement in nano finishes.
Introduction
History
Definition
Types of H bond
Hydrogen bond in water
Bifurcated and over - Coordinated hydrogen bond in water
Hydrogen bonds in DNA and proteins
Hydrogen bonds in polymers
Systematic hydrogen bond
Importance of hydrogen bond
Conclusion
References
Conducting polymers are those polymers which conduct electricity due to extended P- orbital system. Due to this extension of P orbital electrons can move from one end to another end of the polymer.
Size and coating of nanoparticle have effect on their thermodynamic intreaction with proteins
1. Size and coating of nanoparticles have effect on
their thermodynamic interaction with proteins
Seyed Mohammad Motevalli
Fall 2014
1
Shahid Beheshti University
IRAN
3. 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.
4. 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.
5. Nanoparticle features:
Coating
• 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
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.
6. • 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.
7. Protein features:
Charge
• 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
7
• K. H. R. Choo 2008.
• M. Mahmoudi et al. 2011.
8. Protein features:
Hydrophobicity
• Globular proteins have lesser tend to smaller NPs
• Proteins with less than 200 residues usually have more
hydrophobicity
8
• H. Liao et al. 2005.
• J. Klein. 2005.
• Z. Weng et al. 2001.
9. 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.
10. Thermodynamically interaction:
Gibbs free energy
• Hydrophobic amino
acids usually have
more flexibility
• Smaller NPs have
lesser contact positions
than larger NPs
• Free change Gibbs
energy in larger NP-protein
is more than
smaller ones
Δ퐺 = Δ퐻 − 푇Δ푆
10
• G. D. Rose et al. 1985.
• M. Lundqvist et al. 2008.
• J. M. Hayes et al. 2012.