Biodegradable materials based on silk fibroin and keratin.
Wool and silk were dissolved and used for the preparation of blended films. Two systems are proposed: (1) blend films of silk fibroin and keratin aqueous solutions and (2) silk fibroin and keratin dissolved in formic acid. The FTIR spectra of pure films cast from aqueous solutions indicated that the keratin secondary structure mainly consists of alpha-helix and random coil conformations. The IR spectrum of pure SF is characteristic of films with prevalently amorphous structure (random coil conformation). Pure keratin film cast from formic acid shows an increase in the amount of beta-sheet and disordered keratin structures. The FTIR pattern of SF dissolved in formic acid is characteristic of films with prevalently beta-sheet conformations with beta-sheet crystallites embedded in an amorphous matrix. The thermal behavior of the blends confirmed the FTIR results. DSC curve of pure SF is typical of amorphous SF and the curve of pure keratin show the characteristic melting peak of alpha-helices for the aqueous system. These patterns are no longer observed in the films cast from formic acid due to the ability of formic acid to induce crystallization of SF and to increase the amount of beta-sheet structures on keratin. The nonlinear trend of the different parameters obtained from FTIR analysis and DSC curves of both SF/keratin systems indicate that when proteins are mixed they do not follow additives rules but are able to establish intermolecular interactions. Degradable polymeric biomaterials are preferred candidates for medical applications. It was investigated the degradation behavior of both SF/keratin systems by in vitro enzymatic incubation with trypsin. The SF/keratin films cast from water underwent a slower biological degradation than the films cast from formic acid. The weight loss obtained is a function of the amount of keratin in the blend. This study encourages the further investigation of the type of matrices presented here to be applied whether in scaffolds for tissue engineering or as controlled release drug delivery vehicles.
Vasconcelos
Andreia
A
University of Minho, Campus de Azurém, 4800-058 Guimarães, Portugal. andreiav@det.uminho.pt
Freddi
Giuliano
G
Cavaco-Paulo
Artur
A
D000818:Animals; D012831:Bombyx / Q000737:chemistry; D005349:Fibroins / Q000737:chemistry*; D005561:Formates / Q000737:chemistry*; D007633:Keratins / Q000737:chemistry*; D011487:Protein Conformation; D047011:Silk / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties; D013816:Thermodynamics; D014357:Trypsin / Q000378:metabolism*; D014867:Water / Q000737:chemistry*; D014935:Wool / Q000737:chemistry
D005561:Formates; D047011:Silk; C482288:fibroin, silkworm; D014867:Water; C030544:formic acid; D007633:Keratins; D005349:Fibroins; D014357:Trypsin