CAJ | 학술논문

目的观察枝化状聚乙二醇对牛跟腱Ⅰ型胶原结构与构象稳定性的影响.方法以牛跟腱Ⅰ型胶原为原料,以枝化状聚乙二醇为交联剂,在有效交联的前提下,通过测定羟脯氨酸含量观察聚乙二醇交联对胶原酶解稳定性的影响,采用示差扫描量热法(DSC)观察胶原热变性温度,采用圆二色光谱法(CD)观察聚乙二醇对胶原三螺旋构象稳定性的影响.结果枝化状聚乙二醇交联组24 h降解率为26.79%,而对照组则达97.39%,两者比较差异有统计学意义(P＜0.05).交联组热变性温度为(79.1±1.2)℃,与对照组(68.6±1.9)℃比较,差异有统计学意义(P＜0.05);CD谱测定特征性吸收峰差异无统计学意义(P＞0.05).结论枝化状聚乙二醇可显著提高其热变形温度和抗酶性分解能力,而对其三螺旋结构与构象无明显不利影响,是较理想的生物高分子交联剂,可有望用于胶原分子的交联改性.
목적 관찰지화상취을이순대우근건Ⅰ형효원결구여구상은정성적영향.방법 이우근건Ⅰ형효원위원료,이지화상취을이순위교련제,재유효교련적전제하,통과측정간포안산함량관찰취을이순교련대효원매해은정성적영향,채용시차소묘량열법(DSC)관찰효원열변성온도,채용원이색광보법(CD)관찰취을이순대효원삼라선구상은정성적영향.결과 지화상취을이순교련조24 h강해솔위26.79%,이대조조칙체97.39%,량자비교차이유통계학의의(P＜0.05).교련조열변성온도위(79.1±1.2)℃,여대조조(68.6±1.9)℃비교,차이유통계학의의(P＜0.05);CD보측정특정성흡수봉차이무통계학의의(P＞0.05).결론 지화상취을이순가현저제고기열변형온도화항매성분해능력,이대기삼라선결구여구상무명현불리영향,시교이상적생물고분자교련제,가유망용우효원분자적교련개성.
Objective The triple helix of collagen is the basis of its biological function, such as cell adhesion and tissue remodeling. Crosslinking of collagen with chemical agent will improve the biomechanical properties. However, the effects of differernt crosslinking agents on the structure and conformation stability of type Ⅰ collagen are rarely investigated. Methods The branched polyethylene glycol ( PEG)derivative ( MW 12 kD) was used as crosslinking agent, and allowed to react with bovine achilles' s tendon type Ⅰ collagen modified by succinimidylacetylthioacetate (SATA). The ability of resistance of crosslinked collagen to enzymatic degradation was investigated by measuring the release of hydroxyproline, and differential scanning calorimeter ( DSC ) was taken to determine the thermal denaturation temperature. The effect of PEG on the riple helix of collagen was studied by circular dichroism ( CD) . Results The resistance ability of PEG crosslinked collagen was strongly enhanced when compared with that of control group ( P ＜0. 05 ) , and the thermal denaturation temperature was also significantly rised. CD demonstrated that PEG crosslinking did not result in the destruction of the triple helix conformation of type Ⅰ collagen. Conclusion Branched PEG derivative used in this study is a promising polymer crosslinking agent that may be utilized in the modification of type Ⅰ collagen.