Lactoferrin Circular Dichroism Spectroscopy

Lactoferrin is a natural protein found in the milk of mammals, especially in colostrum. It belongs to the transferrin family, and its main function is to efficiently bind and transport iron ions. In addition to this, lactoferrin also has a wide range of biological activities, including antibacterial, antiviral, anti-inflammatory, and immune system regulation. These activities make lactoferrin important for applications in the food industry, nutritional supplements, and medical fields. The structure and function of lactoferrin are affected by its iron saturation and glycosylation levels. Therefore, studying its structure is crucial for understanding its biological functions.

 

Application of Circular Dichroism (CD) in Lactoferrin Research

Circular dichroism (CD) is a technique for analyzing protein secondary structure by measuring the difference in absorption of polarized light at specific wavelengths. In lactoferrin research, CD is widely used to analyze changes in its secondary structure, especially under different iron saturation and environmental conditions. This includes the content and conformation of secondary structural elements such as α-helices, β-folds, and random coils. Researchers can observe structural changes in lactoferrin during iron binding and release through CD, thus revealing its functional mechanisms. In addition, CD analysis also helps to study the thermal stability and pH stability of lactoferrin, which is important for the processing and storage of lactoferrin in food and medical applications.