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Spider silk is spun in a complex and unique process, thought to depend on a hydrophobic conversion of a predominantly disordered to a beta-sheet rich protein structures. To test this hypothesis we monitored the effect of cationic (DOTAC) and anionic (alkyl sulfate) detergents and of (ii) solvent polarity using a series of alcohols on the secondary structure transition in dilute solutions of native spidroin. Our results showed that the detergents hydrophilic head charge and hydrophobic tail length cooperatively induced either a transition to the beta-sheet rich form or a stable helical state. Changing the solvent polarity showed that HFIP and TFE induced formation of stable helical forms whereas MeOH, EtOH and IsoP induced a kinetically driven formation of beta-sheet rich structure.

Original publication




Journal article


Int J Biol Macromol

Publication Date





215 - 224


2-Propanol, Alcohols, Animals, Anions, Binding Sites, Cations, Circular Dichroism, Detergents, Ethanol, Fibroins, Insect Proteins, Kinetics, Methanol, Protein Conformation, Protein Folding, Protein Structure, Secondary, Quaternary Ammonium Compounds, Silk, Solvents, Spiders, Sulfates, Thermodynamics, Time Factors