Coiled-coil scallops (Chlamys farreri) peptide hydrogel with metal ionic and temperature tunable assembly

• Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farreri protein hydrolysates were studied. According to self-assembled theory, the presence of isoleucine at position 'a' and leucine at 'd' causes a switch between coiled-coil structures. Compared to P-2-CG, the components of & alpha;-helix (23.60 & PLUSMN; 0.56%) were changed into 8-sheet (4.83 & PLUSMN; 2.86%) in the secondary structure of the hydrogel induced by ZnCl2. NMR siginals appeared at high field,which indicated hydrogen bonds were formed between P-2-CG and solvent environments at 20 degrees C. With temperature going up, the hydrogen bonds were broken and nanofibrils were changed into dense aggre-gates. We expected that P-2-CG could provide a new candidate for preparing metal-induced nanofibers or hydrogels with further applications in food industry.

Ämnesord

TEKNIK OCH TEKNOLOGIER  -- Kemiteknik -- Polymerteknologi (hsv//swe)

ENGINEERING AND TECHNOLOGY  -- Chemical Engineering -- Polymer Technologies (hsv//eng)

Nyckelord

Chlamys farreri

Peptide

Hydrogel

Ionic responsive

Temperature responsive

Self-assembly

Publikations- och innehållstyp

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