Abstract:
:Spider aciniform (or wrapping) silk is the toughest of the seven types of spider silks/glue due to a combination of high elasticity and strength. Like most spider silk proteins (spidroins), aciniform spidroin (AcSp1) has a large core repetitive domain flanked by relatively short N- and C-terminal nonrepetitive domains (the NTD and CTD, respectively). The major ampullate silk protein (MaSp) CTD has been shown to control protein solubility and fiber formation, but the aciniform CTD function remains unknown. Here, we compare fiber mechanical properties, solution-state structuring, and fibrous state secondary structural composition, and orientation relative to native aciniform silk for two AcSp1 repeat units with or without fused AcSp1- and MaSp-derived CTDs alongside three AcSp1 repeat units without a CTD. The native AcSp1 CTD uniquely modulated fiber mechanical properties, relative to all other constructs, directly correlating to a native-like structural transformation and alignment.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Xu L,Lefèvre T,Orrell KE,Meng Q,Auger M,Liu XQ,Rainey JKdoi
10.1021/acs.biomac.7b01057subject
Has Abstractpub_date
2017-11-13 00:00:00pages
3678-3686issue
11eissn
1525-7797issn
1526-4602journal_volume
18pub_type
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