乳铁蛋白
化学
肽
离子强度
抗菌肽
氨基酸
抗菌剂
生物化学
先天免疫系统
有机化学
水溶液
受体
作者
Jan G. M. Bolscher,Regina Adão,Kamran Nazmi,Petra A.M. van den Keybus,Wim van ’t Hof,A. van Nieuw Amerongen,Margarida Bastos,E.C.I. Veerman
出处
期刊:Biochimie
[Elsevier]
日期:2009-01-01
卷期号:91 (1): 123-132
被引量:85
标识
DOI:10.1016/j.biochi.2008.05.019
摘要
The innate immunity factor lactoferrin harbours two antimicrobial moieties, lactoferricin and lactoferrampin, situated in close proximity in the N1 domain of the molecule. Most likely they cooperate in many of the beneficial activities of lactoferrin. To investigate whether chimerization of both peptides forms a functional unit we designed a chimerical structure containing lactoferricin amino acids 17–30 and lactoferrampin amino acids 265–284. The bactericidal activity of this LFchimera was found to be drastically stronger than that of the constituent peptides, as was demonstrated by the need for lower dose, shorter incubation time and less ionic strength dependency. Likewise, strongly enhanced interaction with negatively charged model membranes was found for the LFchimera relative to the constituent peptides. Thus, chimerization of the two antimicrobial peptides resembling their structural orientation in the native molecule strikingly improves their biological activity.
科研通智能强力驱动
Strongly Powered by AbleSci AI