抗菌乳铁蛋白肽:隐藏在多功能蛋白保护功能中的玩家。

International Journal of Peptides Pub Date : 2013-01-01 Epub Date: 2013-02-13 DOI:10.1155/2013/390230
Mau Sinha, Sanket Kaushik, Punit Kaur, Sujata Sharma, Tej P Singh
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引用次数: 104

摘要

乳铁蛋白是一种多功能的铁结合糖蛋白,它显示出广泛的作用模式来执行其主要的抗菌功能。它含有各种抗菌肽,这些肽在蛋白酶水解后释放出来。这些肽显示出与自然界中发现的抗菌阳离子肽的相似性。在当前抗生素耐药性增加的情况下,有必要发现新的抗微生物药物。在此背景下,对乳铁蛋白n叶抗菌肽的结构和功能进行了综述。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的结构特性的种间比较。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Antimicrobial lactoferrin peptides: the hidden players in the protective function of a multifunctional protein.

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.

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