Bioinspired artificial protein materials: Self-assembly and order from nano to macroscale

Min Dai; Jennifer S. Haghpanah; Carlo Yuvienco; Jin Kim Montclare

doi:10.1557/opl.2011.471

Bioinspired artificial protein materials: Self-assembly and order from nano to macroscale

Min Dai, Jennifer S. Haghpanah, Carlo Yuvienco, Jin Kim Montclare

Chemical and Biomolecular Engineering

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

Abstract

We describe the biosynthesis and characterization of protein materials comprised of two distinct self-assembling domains (SADs): elastin (E) found in tissue for its elastic properties and cartilage oligomeric matrix protein coiled-coil (COMPcc, C) predominantly located in joint and in bones. Based on earlier studies on protein block polymers comprised these two SADs, orientation and number of blocks play a crucial role in the overall stimuli-responsive supramolecular assembly behavior. Here we fabricate a range of E _nC and CE _n block polymers in which the E domain is systematically truncated to explore the effects of the E domain on the overall physicochemical behavior.

Original language	English (US)
Title of host publication	Soft Matter, Biological Materials and Biomedical Materials - Synthesis, Characterization and Applications
Pages	155-159
Number of pages	5
DOIs	https://doi.org/10.1557/opl.2011.471
State	Published - 2011
Event	2010 MRS Fall Meeting - Boston, MA, United States Duration: Nov 29 2010 → Dec 3 2010

Publication series

Name	Materials Research Society Symposium Proceedings
Volume	1301
ISSN (Print)	0272-9172

Other

Other	2010 MRS Fall Meeting
Country/Territory	United States
City	Boston, MA
Period	11/29/10 → 12/3/10

ASJC Scopus subject areas

General Materials Science
Condensed Matter Physics
Mechanics of Materials
Mechanical Engineering

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10.1557/opl.2011.471

Cite this

Dai, M., Haghpanah, J. S., Yuvienco, C., & Montclare, J. K. (2011). Bioinspired artificial protein materials: Self-assembly and order from nano to macroscale. In Soft Matter, Biological Materials and Biomedical Materials - Synthesis, Characterization and Applications (pp. 155-159). (Materials Research Society Symposium Proceedings; Vol. 1301). https://doi.org/10.1557/opl.2011.471

Bioinspired artificial protein materials: Self-assembly and order from nano to macroscale. / Dai, Min; Haghpanah, Jennifer S.; Yuvienco, Carlo et al.
Soft Matter, Biological Materials and Biomedical Materials - Synthesis, Characterization and Applications. 2011. p. 155-159 (Materials Research Society Symposium Proceedings; Vol. 1301).

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

Dai, M, Haghpanah, JS, Yuvienco, C & Montclare, JK 2011, Bioinspired artificial protein materials: Self-assembly and order from nano to macroscale. in Soft Matter, Biological Materials and Biomedical Materials - Synthesis, Characterization and Applications. Materials Research Society Symposium Proceedings, vol. 1301, pp. 155-159, 2010 MRS Fall Meeting, Boston, MA, United States, 11/29/10. https://doi.org/10.1557/opl.2011.471

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abstract = "We describe the biosynthesis and characterization of protein materials comprised of two distinct self-assembling domains (SADs): elastin (E) found in tissue for its elastic properties and cartilage oligomeric matrix protein coiled-coil (COMPcc, C) predominantly located in joint and in bones. Based on earlier studies on protein block polymers comprised these two SADs, orientation and number of blocks play a crucial role in the overall stimuli-responsive supramolecular assembly behavior. Here we fabricate a range of E nC and CE n block polymers in which the E domain is systematically truncated to explore the effects of the E domain on the overall physicochemical behavior.",

author = "Min Dai and Haghpanah, {Jennifer S.} and Carlo Yuvienco and Montclare, {Jin Kim}",

note = "Funding Information: This work was supported by the AFOSR (FA-9550-07-1-0060 to J.K.M.), ARO (W911NF-10-1-0228), in part by the NSF MRSEC Program under Awards Number DMR-0820341, the Society of Plastic Engineers (J.S.H.) and GK-12 Fellows grant DGE-0741714 (J.S.H., C.Y.).; 2010 MRS Fall Meeting ; Conference date: 29-11-2010 Through 03-12-2010",

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AB - We describe the biosynthesis and characterization of protein materials comprised of two distinct self-assembling domains (SADs): elastin (E) found in tissue for its elastic properties and cartilage oligomeric matrix protein coiled-coil (COMPcc, C) predominantly located in joint and in bones. Based on earlier studies on protein block polymers comprised these two SADs, orientation and number of blocks play a crucial role in the overall stimuli-responsive supramolecular assembly behavior. Here we fabricate a range of E nC and CE n block polymers in which the E domain is systematically truncated to explore the effects of the E domain on the overall physicochemical behavior.

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Bioinspired artificial protein materials: Self-assembly and order from nano to macroscale

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