期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 139, 期 10, 页码 3796-3804出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.6b13146
关键词
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资金
- Biomaterials Program of the U.S. National Science Foundation [DMR-1506483]
- National Science Foundation Graduate Research Fellowship [DGE-1141169]
- HHMI Gilliam Fellowship
- Division Of Materials Research
- Direct For Mathematical & Physical Scien [1506483] Funding Source: National Science Foundation
Coiled-coil domains can direct the assembly of protein block copolymers into physically cross-linked, viscoelastic hydrogels. Here, we describe the use of fluorescence recovery after photobleaching (FRAP) to probe chain mobility in reversible hydrogels assembled from engineered proteins bearing terminal coiled-coil domains. We show that chain mobility can be related to the underlying dynamics of the coiled-coil domains by application of a three-state hopping model of chain migration. We further show that genetic programming allows the effective mobility of network chains to be varied 500 -fold through modest changes in protein sequence. Destabilization of the coiled-coil domains by site-directed mutagenesis increases the effective diffusivity of probe chains. Conversely, probe mobility is reduced by expanding the hydrophobic surface area of the coiled-coil domains through introduction of the bulky leucine surrogate homoisoleucine. Predictions from the three-state model imply asymmetric sequential binding of the terminal domains. Brownian Dynamics simulations suggest that binding asymmetry is a general feature of reversible gels, arising from a loss in entropy as chains transition to a conformationally restricted bridged state.
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