title: Rational design of responsive self-assembling peptides from native protein sequences.
abstract: This study used identified functional native domains from spider flagelliform silk protein and the Ca(2+) binding domain of lipase Lip A from Serratia marcescens . After carefully comparing the primary structures of both sequences, we rationally designed a newly sequenced eD(2) by "hiding" the ion binding sequence in the silk structure sequence. This helped avoid redundancy, and the new sequence had properties of both model sequences. In water, eD(2) formed uniform spherical agglomerates with a β-spiral structure. Triggered by Ca(2+), eD(2) formed nanofibers with higher compliance and thermal stability. We demonstrated the specialties of this novel peptide design by changing the pH, using other metal ions, and mutating the model sequence.
authors.affiliation: Bio-Materials and Technology Lab, Department of Grain Science and Industry, Kansas State University, Manhattan, Kansas 66506, United States.
authors.forename: Hongzhou
authors.initials: H
authors.lastname: Huang
authors.forename: Xiuzhi S
authors.initials: XS
authors.lastname: Sun
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002118:Calcium; D015195:Drug Design; D006358:Hot Temperature; D057139:Nanofibers / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D055550:Protein Stability; D017433:Protein Structure, Secondary; D047011:Silk / Q000737:chemistry*; D013112:Spiders
chemical_list: D010446:Peptide Fragments; D047011:Silk; D002118:Calcium