Sinha Mau, Kaushik Sanket, Kaur Punit, Sharma Sujata, Singh Tej P
Department of Biophysics, All India Institute of Medical Sciences, Ansari Nagar, New Delhi 110029, India.
Int J Pept. 2013;2013:390230. doi: 10.1155/2013/390230. Epub 2013 Feb 13.
Lactoferrin is a multifunctional, iron-binding glycoprotein which displays a wide array of modes of action to execute its primary antimicrobial function. It contains various antimicrobial peptides which are released upon its hydrolysis by proteases. These peptides display a similarity with the antimicrobial cationic peptides found in nature. In the current scenario of increasing resistance to antibiotics, there is a need for the discovery of novel antimicrobial drugs. In this context, the structural and functional perspectives on some of the antimicrobial peptides found in N-lobe of lactoferrin have been reviewed. This paper provides the comparison of lactoferrin peptides with other antimicrobial peptides found in nature as well as interspecies comparison of the structural properties of these peptides within the native lactoferrin.
乳铁蛋白是一种多功能的铁结合糖蛋白，它展现出多种作用方式来执行其主要的抗菌功能。它包含各种抗菌肽，这些抗菌肽在被蛋白酶水解时会释放出来。这些肽与自然界中发现的抗菌阳离子肽具有相似性。在当前抗生素耐药性不断增加的情况下，需要发现新型抗菌药物。在此背景下，对乳铁蛋白N叶中发现的一些抗菌肽的结构和功能观点进行了综述。本文提供了乳铁蛋白肽与自然界中发现的其他抗菌肽的比较，以及这些肽在天然乳铁蛋白内结构特性的种间比较。
