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Collagen functionalized with unsaturated cyclic anhydrides—interactions in solution and solid state
Author(s) -
Potorac S.,
Popa M.,
Picton L.,
Dulong V.,
Verestiuc L.,
Cerf D. Le
Publication year - 2014
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22319
Subject(s) - chemistry , maleic anhydride , thixotropy , polymer chemistry , triple helix , aqueous solution , covalent bond , random coil , swelling , polymer , chemical engineering , organic chemistry , crystallography , stereochemistry , circular dichroism , engineering , copolymer
Maleic anhydride (CMA) and itaconic anhydride modified collagen (CITA) were prepared as precursors for production of interpenetrated polymer networks (IPN). Calculated values for Huggins coefficient in aqueous diluted and semi‐diluted solutions of modified collagen indicated a slightly tendency of aggregation for itaconic anhydride‐modified collagen. In semi‐diluted solution collagen (Coll) and CMA present slightly differences in the thixotropic behavior, while CITA has a pronounced thixotropic behavior. Flow and oscillatory measurements revealed an elastic behavior of the collagen solutions, pure and modified with MA or ITA, as the storage modulus ( G ′) has always a superior value compared with the loss modulus ( G ″). The denaturation temperature ( T d ) of unmodified collagen increased from 34 o C to 40 o C for CMA and to 39 o C for CITA respectively, by formation of covalent bonds that stabilize the triple helix. © 2013 Wiley Periodicals, Inc. Biopolymers 101: 228–236, 2014.