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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Role of polyalanine domains in beta-sheet formation in spider silk block copolymers
Olena S Rabotyagova1, Peggy Cebe, David L Kaplan
1Department of Biomedical Engineering, Tufts University, Medford, Massachusetts 02155, USA.
Abstract:
Genetically engineered spider silk-like block copolymers were studied to determine the influence of polyalanine domain size on secondary structure. The role of polyalanine block distribution on beta-sheet formation was explored using FT-IR and WAXS. The number of polyalanine blocks had a direct effect on the formation of crystalline beta-sheets, reflected in the change in crystallinity index as the blocks of polyalanines increased. WAXS analysis confirmed the crystalline nature of the sample with the largest number of polyalanine blocks. This approach provides a platform for further exploration of the role of specific amino acid chemistries in regulating the assembly of beta-sheet secondary structures, leading to options to regulate material properties through manipulation of this key component in spider silks.
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