Design, Engineering and Discovery of Novel α-Helical and β-Boomerang Antimicrobial Peptides against Drug Resistant Bacteria

被引:51
作者
Bhattacharjya, Surajit [1 ]
Straus, Suzana K. [2 ]
机构
[1] Nanyang Technol Univ, Sch Biol Sci, 60 Nanyang Dr, Singapore 637551, Singapore
[2] Univ British Columbia, Dept Chem, 2036 Main Mall, Vancouver, BC V6T 1Z1, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
multi-drug resistant (MDR) bacteria; extensively drug resistant (XDR) bacteria; antimicrobial peptides (AMPs); lipopolysaccharide (LPS) binding; alpha-helical and beta-boomerang AMPs; HOST-DEFENSE PEPTIDES; GRAM-NEGATIVE BACTERIA; AMINO-ACID SUBSTITUTION; ACTIVE AUREIN PEPTIDES; FROGS LITORIA-AUREA; TEMPORIN-L; LIPOPOLYSACCHARIDE MICELLES; MEMBRANE-PERMEABILIZATION; NMR STRUCTURES; IN-VITRO;
D O I
10.3390/ijms21165773
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In an era where the pipeline of new antibiotic development is drying up, the continuous rise of multi-drug resistant (MDR) and extensively drug resistant (XDR) bacteria are genuine threats to human health. Although antimicrobial peptides (AMPs) may serve as promising leads against drug resistant bacteria, only a few AMPs are in advanced clinical trials. The limitations of AMPs, namely their low in vivo activity, toxicity, and poor bioavailability, need to be addressed. Here, we review engineering of frog derived short alpha-helical AMPs (aurein, temporins) and lipopolysaccharide (LPS) binding designed beta-boomerang AMPs for further development. The discovery of novel cell selective AMPs from the human proprotein convertase furin is also discussed.
引用
收藏
页码:1 / 22
页数:21
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