title: Structural properties of pepsin-solubilized collagen acylated by lauroyl chloride along with succinic anhydride.
abstract: The structural properties of pepsin-solubilized calf skin collagen acylated by lauroyl chloride along with succinic anhydride were investigated in this paper. Compared with native collagen, acylated collagen retained the unique triple helix conformation, as determined by amino acid analysis, circular dichroism and X-ray diffraction. Meanwhile, the thermostability of acylated collagen using thermogravimetric measurements was enhanced as the residual weight increased by 5%. With the temperature increased from 25 to 115 °C, the secondary structure of native and acylated collagens using Fourier transform infrared spectroscopy measurements was destroyed since the intensity of the major amide bands decreased and the positions of the major amide bands shifted to lower wavenumber, respectively. Meanwhile, two-dimensional correlation spectroscopy revealed that the most sensitive bands for acylated and native collagens were amide I and II bands, respectively. Additionally, the corresponding order of the groups between native and acylated collagens was different and the correlation degree for acylated collagen was weaker than that of native collagen, suggesting that temperature played a small influence on the conformation of acylated collagen, which might be concluded that the hydrophobic interaction improved the thermostability of collagen.
authors.affiliation: The Key Laboratory of Leather Chemistry and Engineering of Ministry of Education, Sichuan University, Chengdu 610065, PR China; College of Life Sciences, Anqing Normal University, Anqing 246011, PR China.
authors.forename: Conghu
authors.initials: C
authors.lastname: Li
authors.affiliation: The Key Laboratory of Leather Chemistry and Engineering of Ministry of Education, Sichuan University, Chengdu 610065, PR China.
authors.forename: Zhenhua
authors.initials: Z
authors.lastname: Tian
authors.affiliation: The Key Laboratory of Leather Chemistry and Engineering of Ministry of Education, Sichuan University, Chengdu 610065, PR China.
authors.forename: Wentao
authors.initials: W
authors.lastname: Liu
authors.affiliation: The Key Laboratory of Leather Chemistry and Engineering of Ministry of Education, Sichuan University, Chengdu 610065, PR China. Electronic address: liguoyings@163.com.
authors.forename: Guoying
authors.initials: G
authors.lastname: Li
mesh_terms: D000215:Acylation; D000596:Amino Acids / Q000032:analysis; D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry*; D007850:Lauric Acids / Q000737:chemistry; D010434:Pepsin A / Q000737:chemistry*; D011487:Protein Conformation; D017550:Spectroscopy, Fourier Transform Infrared; D013387:Succinic Anhydrides / Q000737:chemistry; D013696:Temperature; D013818:Thermogravimetry; D014961:X-Ray Diffraction
chemical_list: D000596:Amino Acids; D007850:Lauric Acids; D013387:Succinic Anhydrides; C031801:succinic anhydride; D003094:Collagen; D010434:Pepsin A
keywords: Acylation; Lauroyl chloride; Pepsin-solubilized collagen; Structural properties; Succinic anhydride