Diamines prevent thermal aggregation and inactivation of lysozyme
Diamines prevent thermal aggregation and inactivation of lysozyme
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DOI：
10.1263/jbb.100.556
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发表时间：
2005-11-01
影响因子：
2.8
通讯作者：
Takagi, M
中科院分区：
文献类型：
--
作者：
Okanojo, M;Shiraki, K;Takagi, M
蛋白质聚集是涉及蛋白质的生物应用和生物医学领域的主要障碍。在这项研究中，我们研究了作为化学伴侣的小添加剂的基本结构。聚集抑制主管添加剂1，3-二氨基丙烷，1，4-二氨基丁烷，和1，5-二氨基戊烷，抑制聚集在给定的顺序，而没有二醇或单胺防止热聚集和灭活的溶菌酶。溶菌酶与1，3-丙二胺的热活化率与溶菌酶与精胺和精氨酸乙酯的热活化率几乎相同，这是迄今报道的最突出的添加剂。
Protein aggregation is a major obstacle in both biological applications and biomedical fields involving proteins. In this study, we investigated the essential structure of small additives that function as chemical chaperones. Aggregation-suppressing competent additives were 1,3-diaminopropane, 1,4-diaminobutane, and 1,5-diaminopentane, which suppressed aggregation in the given order; whereas no diols or monoamines prevented the thermal aggregation and the inactivation of lysozyme. The heat-in activation rate of lysozyme with 1,3-diaminopropane was almost identical to that of lysozyme with spermine and arginine ethylester, which are the most prominent additives reported yet.