Disulfide Bridges in Defensins

作者：Zhao, Bing-Chuan; Lin, Hua-Can; Yang, Dan; Ye, Xiyang; Li, Zi-Gang^*

来源：Current Topics in Medicinal Chemistry, 2016, 16(2): 206-219.

DOI：10.2174/1568026615666150701115911

• Antibiotics
• beta-hairpin structure
• Chemotactic activity
• Defensin
• disulfide bond
• structure-function relationship
• Truncated peptide

Defensins are small cationic cysteine rich peptides, which usually contain 18-45 amino acids and possess amphiphilic properties. The term "defensin" was coined as the sequences of rabbit and human leukin/phagocytin molecules were first reported in 1985. Since then, various defensins were isolated and characterized from insects, plants and vertebrates. Using vertebrate defensins as examples, defensins are categorized into three sub-families based on their different patterns of intramolecular disulfide linkages: alpha defensins, beta defensins, and theta defensins. During the past decades, continuous attentions were casted on various defensins for their broad activity against bacteria, fungi and viruses. In this review, we focus on the effect of characteristic intramolecular disulfide bonds on the antimicrobial activity of defensins. The disulfide bonds are important for holding the defensins in their three dimensional structures, while also contribute to their antimicrobial activity and chemotactic activity. This review summarizes the effects of disulfide bonds, their synthetic formation pathways and potential pharmaceutical applications.

• 出版日期2016
• 单位北京大学深圳研究生院; 暨南大学; 北京大学