Academic Journal

Dependence of Self-Assembled Peptide Hydrogel Network Structure on Local Fibril Nanostructure

التفاصيل البيبلوغرافية
العنوان: Dependence of Self-Assembled Peptide Hydrogel Network Structure on Local Fibril Nanostructure
المؤلفون: Hule, Rohan A., Nagarkar, Radhika P., Hammouda, Boualem, Schneider, Joel P., Pochan, Darrin J.
المصدر: Macromolecules, 42(18), 7137-7145, (2009-09-22)
بيانات النشر: American Chemical Society
سنة النشر: 2009
المجموعة: Caltech Authors (California Institute of Technology)
الوصف: Physically cross-linked, fibrillar hydrogel networks are formed by the self-assembly of β-hairpin peptide molecules with varying degrees of strand asymmetry. The peptide registry in the self-assembled state can be used as a design element to generate fibrils with twisting, nontwisting, or laminated morphology. The mass density of the networks varies significantly, and can be directly related to the local fibrillar morphology as evidenced by small angle neutron scattering (SANS) and in situ substantiation using cryogenic transmission electron microscopy (cryo-TEM) under identical concentrations and conditions. Similarly, the density of the network is dependent on changes in the peptide concentration. Bulk rheological properties of the hydrogels can be correlated to the fibrillar nanostructure, with the stiffer, laminated fibrils forming networks with a higher G′ as compared to the flexible, singular fibrillar networks. ; © 2009 American Chemical Society. Received February 12, 2009; Revised Manuscript Received July 16, 2009. The identification of any commercial product or trade name does not imply endorsement or recommendation by the National Institute of Standards and Technology. This work was supported byNSFCHE0348323 (JPS-RPN), a Small Angle Neutron Scattering on Polymers and Complex Fluids Award (DJP-RAH, US Department of Commerce, # 70NANB7H6178), NIH 5RO1DEO16383, and the W. M. Keck Foundation for funding the College of Engineering Electron Microscopy Laboratory. This work utilized facilities supported in part by the National Science Foundation under Agreement No. DMR-0454672. Supporting Information Available: Cryo-TEM image analysis and AFM data with image analysis. This material is available free of charge via the Internet at http://pubs.acs.org. ; Supplemental Material - Hule2009p5968Macromolecules_supp.pdf
نوع الوثيقة: article in journal/newspaper
اللغة: unknown
Relation: https://doi.org/10.1021/ma9003242; eprintid:16150
DOI: 10.1021/ma9003242
الاتاحة: https://doi.org/10.1021/ma9003242
Rights: info:eu-repo/semantics/openAccess ; Other
رقم الانضمام: edsbas.53F97F6C
قاعدة البيانات: BASE