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’Mechanical Engineering’ of Elastomeric Proteins: Toward Designing New Protein Building Blocks for Biomaterials

Title’Mechanical Engineering’ of Elastomeric Proteins: Toward Designing New Protein Building Blocks for Biomaterials
Publication TypeJournal Article
Year of Publication2008
AuthorsLi, HB
JournalAdvanced Functional Materials
Volume18
Pagination2643-2657
Date PublishedSep
Type of ArticleReview
ISBN Number1616-301X
KeywordsATOMIC-FORCE MICROSCOPY, BIOLOGICAL ROLES, DIHYDROFOLATE-REDUCTASE, EXTRACELLULAR-MATRIX PROTEIN, FLUORESCENT PROTEIN, IG DOMAIN, MOLECULAR-DYNAMICS SIMULATIONS, PROTEIN, SINGLE, TITIN IMMUNOGLOBULIN DOMAINS, UNFOLDING PATHWAYS
Abstract

Elastomeric proteins are subject to stretching force under biological settings and play important roles in regulating the mechanical properties of a wide range of biological machinery. Elastomeric proteins also underlie the superb mechanical properties of many protein-based biomaterials. The developments of single molecule force spectroscopy have enabled the direct characterization of the mechanical properties of elastomeric proteins at the single molecule level and led to the new burgeoning field of research: single protein mechanics-and engineering. Combined, single molecule atomic force microscopy and protein engineering efforts are well under way to understand molecular determinants for the mechanical stability of elastomeric proteins and to develop methodologies to tune the mechanical properties of proteins in a rational and systematic fashion, which will lead to the ’mechanical engineering’ of elastomeric proteins. Here the current status of these experimental efforts is discussed and the successes and challenges in constructing novel proteins with tailored nanomechanical proteins are highlighted. The prospect of employing such engineered artificial elastomeric proteins as building blocks for the construction of biomaterials for applications ranging from material sciences to biomedical engineering is also discussed.

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