Abstract:
:Accurate prediction and validation of the assembly of bioinspired peptide sequences into fibers with defined mechanical characteristics would aid significantly in designing and creating materials with desired properties. This process may also be utilized to provide insight into how the molecular architecture of many natural protein fibers is assembled. In this work, computational modeling and experimentation are used in tandem to determine how peptide terminal modification affects a fiber-forming core domain. Modeling shows that increased terminal molecular weight and hydrophilicity improve peptide chain alignment under shearing conditions and promote consolidation of semicrystalline domains. Mechanical analysis shows acute improvements to strength and elasticity, but significantly reduced extensibility and overall toughness. These results highlight an important entropic function that terminal domains of fiber-forming peptides exhibit as chain alignment promoters, which ultimately has notable consequences on the mechanical behavior of the final fiber products.
journal_name
Macromol Bioscijournal_title
Macromolecular bioscienceauthors
Jacobsen MM,Tokareva OS,Ebrahimi D,Huang W,Ling S,Dinjaski N,Li D,Simon M,Staii C,Buehler MJ,Kaplan DL,Wong JYdoi
10.1002/mabi.201700095subject
Has Abstractpub_date
2017-09-01 00:00:00issue
9eissn
1616-5187issn
1616-5195journal_volume
17pub_type
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