Detection and Classification of Related Lipopolysaccharides via a Small Array of Immobilized Antimicrobial Peptides

2012 ◽  
Vol 84 (17) ◽  
pp. 7359-7366 ◽  
Author(s):  
Joshua R. Uzarski ◽  
Charlene M. Mello
2021 ◽  
Vol 8 ◽  
Author(s):  
Tao Gong ◽  
Jie Fu ◽  
Lexuan Shi ◽  
Xin Chen ◽  
Xin Zong

Animal antimicrobial peptides (AMPs), known as broad-spectrum and high-efficiency antibacterial activity, are important effector molecules in innate immune system. AMPs not only have antimicrobial, antiviral and antitumor effects but also exhibit important effects in vivo, such as anti-inflammatory response, recruiting immune cells, promoting epithelial damage repair, and promoting phagocytosis of bacteria. However, research on the application of AMPs is incomplete and controversial. This review mainly introduces the classification of AMPs, biological functions, as well as the mechanisms of action, expression rules, and nutrition regulation from three perspectives, aiming to provide important information for the application of AMPs.


2015 ◽  
Author(s):  
Francy L. Camacho ◽  
Rodrigo Torres ◽  
Raúl Ramos Pollán

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Hao-Ting Lee ◽  
Chen-Che Lee ◽  
Je-Ruei Yang ◽  
Jim Z. C. Lai ◽  
Kuan Y. Chang

Antimicrobial peptides (AMPs) are potent drug candidates against microbial organisms such as bacteria, fungi, parasites, and viruses. AMPs have abundant sequences and structures, two fundamental resources for bioinformatics researches, but analyses on how they associate with each other are either nonexistent or limited to partial classification and data. We thus present A Database of Anti-Microbial peptides (ADAM), which contains 7,007 unique sequences and 759 structures, to systematically establish comprehensive associations between AMP sequences and structures through structural folds and to provide an easy access to view their relationships. 30 distinct AMP structural fold clusters with more than one structure are detected and about a thousand AMPs are associated with at least one structural fold cluster. According to ADAM, AMP structural folds are limited—AMPs only cover about 3% of the overall protein fold space.


2012 ◽  
Vol 9 (5) ◽  
pp. 1535-1538 ◽  
Author(s):  
Shaini Joseph ◽  
Shreyas Karnik ◽  
Pravin Nilawe ◽  
V. K. Jayaraman ◽  
Susan Idicula-Thomas

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