Solid-state NMR investigation of major and minor ampullate spider silk in the native and hydrated states.
Silks spun from the major (Ma) and minor (Mi) ampullate glands by the spider Nephila clavipes respond to water differently. Specifically, Ma silk supercontracts (shrinks 40-50% in length) while Mi silk does not contract at all when hydrated with water. In the present study, 1H --> 13C cross polarization magic angle spinning (CP-MAS), 13C MAS NMR collected with dipolar decoupling, and two-dimensional wide-line separation spectra are presented on Mi silk in its native and hydrated state and comparisons are made to Ma silk. This combination of NMR data demonstrates that water plasticizes Mi and Ma silk similarly, with an increase in chain dynamics observed in regions containing Gly, Glu, Ser, Tyr, Leu, and a fraction of Ala when the Mi silk is hydrated. Resonances that correspond to the poly(Ala) and poly(Gly Ala) motifs of Ma and Mi silk are predominately rigid indicating that water does not penetrate these beta-sheet domains.
Holland
Gregory P
GP
Magnetic Resonance Research Center, Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287-1604, USA. Greg.holland@asu.edu
Jenkins
Janelle E
JE
Creager
Melinda S
MS
Lewis
Randolph V
RV
Yarger
Jeffery L
JL
D000595:Amino Acid Sequence; D000818:Animals; D005260:Female; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D047011:Silk / Q000032:analysis / Q000737:chemistry* / Q000235:genetics; D013112:Spiders / Q000737:chemistry; D014867:Water / Q000032:analysis / Q000737:chemistry*
D047011:Silk; D014867:Water