Yielding Behavior of Tough Semicrystalline Hydrogels


BILICI C., İDE S., Okay O.

MACROMOLECULES, cilt.50, sa.9, ss.3647-3654, 2017 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 50 Sayı: 9
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1021/acs.macromol.7b00507
  • Dergi Adı: MACROMOLECULES
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.3647-3654
  • İstanbul Teknik Üniversitesi Adresli: Evet

Özet

Supramolecular semicrystalline hydrogels are soft functional materials consisting of water-swollen hydrophilic polymer chains interconnected by hydrophobic segments forming lamellar crystals. Although such hydrogels with high crystallinity are mechanically strong, with elastic moduli and tensile strength of 80-300 MPa and 4-7 MPa, respectively, they are brittle and rupture at a stretch of less than 20% without yielding. Here, we report that the incorporation of a small amount of a weak hydrophobe into semicrystalline hydrogels significantly increases their toughness and stretchability without losing their high modulus and high strength. We design a highly entangled physical network based on poly(N,N-dimethylacrylamide) (PDMA) chains containing n-octadecyl acrylate (C18A) and lauryl methacrylate (C12M) segments chain lengths of 18 and 12 carbons, respectively. By including 0.1-0.4 mol % C12M into the PDMA backbone containing 30 mol % C18A segments, we were able to create more ordered and thinner lamellar crystals with a layered structure. Simultaneously, a brittle-to-ductile transition was observed due to the appearance of necking behavior leading to 10-fold increase of toughness. The significant toughness improvement upon incorporation of C12M into the semicrystalline hydrogels could be explained with the appearance of active tie molecules under external force interconnecting the lamellar clusters. The hydrogels also exhibit reversible tensile deformation induced by heating above the melting temperature of crystalline domains.