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research article

Analytical ultracentrifugation to support the development of biomaterials and biomedical devices

Wandrey, Christine  
•
Hasegawa, Urara
•
van der Vlies, André J
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2011
Methods

Analytical ultracentrifugation (AUC) primarily serves to investigate hydrodynamic and thermodynamic properties of natural and synthetic macromolecules and colloids in solution, dispersion or suspension. Beside such more conventional use, AUC can support materials development particularly by combining different optical systems, if the AUC is equipped with such, or using complementary data evaluation approaches. In this context, an Optima XL-I equipped with absorbance (AO) and interference optics (IO) was used alone or complementary to study the success of conjugation of biopolymers, to evaluate the completeness of the incorporation of macromolecules into micelles and vesicles, and to analyze the composition and homogeneity of macromolecular assemblies. The combination of AO and IO proved covalent binding of concanavalin A to dextran without macromolecular degradation as well as the formation of mixed micelles composed of two types of block copolymers. Further, AUC contributed to analyze the homogeneity, purity, size and size distribution of carbon monoxide-releasing macromolecular assemblies. These case studies revealed that the application possibilities of AUC are by far not completely discovered but can still be extended.

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Type
research article
DOI
10.1016/j.ymeth.2010.12.003
Web of Science ID

WOS:000290649700010

PubMed ID

21146611

Author(s)
Wandrey, Christine  
Hasegawa, Urara
van der Vlies, André J
O'Neil, Conlin
Angelova, Nela
Hubbell, Jeffrey A.  
Date Issued

2011

Published in
Methods
Volume

54

Issue

1

Start page

92

End page

100

Subjects

Analytical ultracentrifugation

•

Biomaterials

•

Biopolymer modification

•

Mixed micelles

•

Macromolecular assemblies

•

Concanavalin-A

•

Sedimentation-Velocity

•

Electron-Microscopy

•

Affinity Sensor

•

Micelles

•

Nanoparticles

•

Glucose

•

Binding

•

Protein

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LMRP  
Available on Infoscience
February 24, 2011
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/64822
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