Preparation and characterization of an advanced collagen aggregate from porcine acellular dermal matrix

被引：60
作者：
Liu, Xinhua [1 ,2 ]
Dan, Nianhua [1 ,2 ]
Dan, Weihua [1 ,2 ]
机构：
[1] Sichuan Univ, Educ Minist, Key Lab Leather Chem & Engn, Chengdu 610065, Sichuan, Peoples R China
[2] Sichuan Univ, Biomed Engn Res Ctr, Chengdu 610065, Sichuan, Peoples R China
来源：
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2016年 / 88卷
基金：
中国国家自然科学基金;
关键词：
Collagen aggregate; Collagen; Structure; CROSS-LINKING; SKIN; FIBRIL; GELATIN; LUMICAN; TISSUES; FIBERS; MODEL; BONE;
D O I：
10.1016/j.ijbiomac.2016.03.066
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The objective of this study was to extract and characterize an advanced collagen aggregate (Ag-col) from porcine acellular dermal matrix (pADM). Based on histological examination, scanning electron microscopy (SEM) and atomic force microscope (AFM), Ag-col was composed of the D-periodic cross striated collagen fibrils and thick collagen fiber bundles with uneven diameters and non-orientated arrangement. Fourier transform infrared (FTIR) spectra of pADM, Ag-col and Col were similar and revealed the presence of the triple helix. Circular dichroism (CD) analysis exhibited a slightly higher content of alpha-helix but inappreciably less amount of random coil structure in Ag-col compared to Col. Moreover, imino acid contents of pADM, Ag-col and Col were 222.43, 218.30 and 190.01 residues/1000 residues, respectively. From zeta potential analysis, a net charge of zero was found at pH 6.45 and 6.11 for Ag-col and Col, respectively. Differential scanning calorimetry (DSC) study suggested that the Td of Ag-col was 20 degrees C higher than that of Col as expected, and dynamic mechanical analysis (DMA) indicated that Ag-col possessed a higher storage modulus but similar loss factor compared to Col. Therefore, the collagen aggregate from pADM could serve as a better alternative source of collagens for further applications in food and biological industries. (C) 2016 Elsevier B.V. All rights reserved.
引用
收藏
页码：179 / 188
页数：10
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