Relationship between structure and function of cathelicidins and their molecular design: a review.

Author: Chen WANG ¹ ; Lan FENG ¹ ; Haining YU ¹ ; Yipeng WANG ²
Author Information

1. School of Life Science and Biotechnology, Dalian University of Technology, Dalian 116024, Liaoning, China.
2. College of Pharmaceutical Sciences, Soochow University, Suzhou 215123, Jiangsu, China.
Publication Type:Journal Article
Keywords: cathelicidins; function; molecular design; stability; structure
From: Chinese Journal of Biotechnology 2017;33(1):27-35
CountryChina
Language:Chinese
Abstract: Cathelicidins play critical roles in mammalian innate immune defense against invasive bacterial infection. In addition to their broad-spectrum bactericidal effect, cathelicidins are interesting peptide-based drug templates because they have multiple functions including anti-inflammatory, wound healing, and angiogenesis promotion. This article summarizes the aim and method of cathelicidin molecular designs. Residue mutation, fragment assembly, chemical modification, and construction of conjugates and dimers are usually used to increase the biological activities. Addition or deletion of certain residues, disruption of leucine zipper and phenylalanine zipper are used to reduce the hemolysis and cytotoxicity. By substituting L-amino acids with D-amino acids, circular constructions and immobilization, cathelicidins' in vitro and in vivo stability could be greatly enhanced, especially their proteinase resistance.