title: Modification of collagen with a natural cross-linker, procyanidin.
abstract: We have investigated the modification of collagen with a natural plant polyphenol, procyanidin under acidic conditions. Fourier transform infrared spectroscopy (FTIR) and Atomic force microscopy (AFM) studies demonstrate that the hydrogen bond interactions between collagen and procyanidin does not destroy the triple helix conformation of collagen, and the fibril aggregation occurs because of the cross-linking with procyanidin. The water contact angle (WCA) tests indicate that the hydrophobicity of the procyanidin modified collagen films can be improved. Whereas, the water vapor permeability (WVP) of the films decrease with the increasing procyanidin content due to the formation of denser structure. Moreover, differential scanning calorimetry (DSC) and thermogravimetric (TG) measurements reveal that the collagen/procyanidin films have improved thermal stability in comparison with pure collagen. The present study reveals that procyanidin stabilizes collagen as a cross-linker and preserves its triple helical structure.
authors.affiliation: Department of Biomass and Leather Engineering, National Engineering Laboratory for Clean Technology of Leather Manufacture, Sichuan University, Chengdu, Sichuan 610065, China.
authors.forename: Lirong
authors.initials: L
authors.lastname: He
authors.forename: Changdao
authors.initials: C
authors.lastname: Mu
authors.forename: Jiabo
authors.initials: J
authors.lastname: Shi
authors.forename: Qian
authors.initials: Q
authors.lastname: Zhang
authors.forename: Bi
authors.initials: B
authors.lastname: Shi
authors.forename: Wei
authors.initials: W
authors.lastname: Lin
mesh_terms: D000818:Animals; D044946:Biflavonoids / Q000737:chemistry*; D002152:Calorimetry, Differential Scanning; D002392:Catechin / Q000737:chemistry*; D002417:Cattle; D003094:Collagen / Q000737:chemistry*; D003432:Cross-Linking Reagents / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D018625:Microscopy, Atomic Force; D010539:Permeability; D044945:Proanthocyanidins / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D013227:Steam; D013696:Temperature
chemical_list: D044946:Biflavonoids; D003432:Cross-Linking Reagents; D044945:Proanthocyanidins; D013227:Steam; C017674:procyanidin; D002392:Catechin; D003094:Collagen