Issue 9, 2010

Supramolecular assembly and small molecule recognition by genetically engineered protein block polymers composed of two SADs

Abstract

Genetically engineered protein block polymers are an important class of biomaterials that have gained significant attention in recent years due to their potential applications in biotechnology, electronics and medicine. The majority of the protein materials have been composed of at least a single self-assembling domain (SAD), enabling the formation of supramolecular structures. Recently, we developed block polymers consisting of two distinct SADs derived from an elastin-mimetic polypeptide (E) and the alpha-helical COMPcc (C). These protein polymers, synthesized as the block sequences—EC, CE, and ECE—were assessed for overall conformation and macroscopic thermoresponsive behavior. Here, we investigate the supramolecular assembly as well as the small molecule binding and release profile of these block polymers. Our results demonstrate that the protein polymers assemble into particles as well as fully or partially networked structures in a concentration dependent manner that is distinct from the individual E and C homopolymers and the E+C non-covalent mixture. In contrast to synthetic block polymers, the structured assembly, binding and release abilities are highly dependent on the composition and orientation of the blocks. These results reveal the promise for these block polymers for therapeutic delivery and biomedical scaffolds.

Graphical abstract: Supramolecular assembly and small molecule recognition by genetically engineered protein block polymers composed of two SADs

Supplementary files

Article information

Article type
Paper
Submitted
03 Feb 2010
Accepted
24 Mar 2010
First published
18 May 2010

Mol. BioSyst., 2010,6, 1662-1667

Supramolecular assembly and small molecule recognition by genetically engineered protein block polymers composed of two SADs

J. S. Haghpanah, C. Yuvienco, E. W. Roth, A. Liang, R. S. Tu and J. K. Montclare, Mol. BioSyst., 2010, 6, 1662 DOI: 10.1039/C002353A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements