Thermodynamics and Kinetics of the Interactions Between Proteins and Hydrophilic Polymers

Timo Schäfer (), Christian Muhl, Matthias Barz, Friederike Schmid and Giovanni Settanni
Additional contact information
Timo Schäfer: Johannes Gutenberg University, Institut für Physik
Christian Muhl: Johannes Gutenberg University, Institut für Organische Chemie
Matthias Barz: Johannes Gutenberg University, Institut für Organische Chemie
Friederike Schmid: Johannes Gutenberg University, Institut für Physik
Giovanni Settanni: Johannes Gutenberg University, Institut für Physik

A chapter in High Performance Computing in Science and Engineering '19, 2021, pp 65-76 from Springer

Abstract: Abstract Hydrophilic polymers are being investigated as possible coating agents for therapeutic nanoparticles because of their capacity to reduce immune response and increase circulation life time. The mechanism of action of these coatings is not well understood although it is clear that they unspecifically reduce the amount of proteins adsorbing on the nanoparticle surface coming in contact with biological fluids. Here we have investigated, using state-of-the-art atomistic molecular dynamics simulations, the equilibrium and kinetic properties of the interactions forming between human serum albumin, the most abundant protein in the blood stream, and two different and promising polymers poly(ethylene glycol) and poly-sarcosine and we have compared the results with a polymer which is an isomer of poly-sarcosine but has a totally different behavior in terms of adsorption, poly-alanine, because of its well-known aggregation propensity. The results show how the two hydrophilic polymers have a very similar behavior in terms of the amount of polymers adsorbed on the protein surface, pattern of interactions and the kinetics of the adsorption process, with differences emerging due to the different flexibility of the two molecules. In contrast poly-alanine adsorbs significantly more strongly on the protein surface, with a slower kinetics, and a quantitatively, but not qualitatively, different interaction pattern with the surface amino acids with respect to the hydrophilic polymers.

Date: 2021
References: Add references at CitEc
Citations:

There are no downloads for this item, see the EconPapers FAQ for hints about obtaining it.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:spr:sprchp:978-3-030-66792-4_4

Ordering information: This item can be ordered from
http://www.springer.com/9783030667924

DOI: 10.1007/978-3-030-66792-4_4

Access Statistics for this chapter

More chapters in Springer Books from Springer
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().