Development of Novel Lipid—Peptide Hybrid Compounds with Antibacterial Activity from Natural Cationic Antibacterial Peptides.

ChemInform ◽  
2004 ◽  
Vol 35 (23) ◽  
Author(s):  
Hyun-Sik Oh ◽  
Seunghee Kim ◽  
Hyeongjin Cho ◽  
Keun-Hyeung Lee
Nanoscale ◽  
2021 ◽  
Author(s):  
Wenlu Tu ◽  
Ke Xue ◽  
Shaofeng Lou ◽  
Chunlei Zhu ◽  
Zhilin Yu

Current strategies for design of antibacterial peptides show limitation in development of assembled antibacterial peptides due to the challenges in simultaneously balancing the antibacterial activity and assembling behavior. Herein, we...


2008 ◽  
Vol 3 (2) ◽  
pp. 203-206
Author(s):  
Rong Peng ◽  
Zhong Yang ◽  
Kaiyu Liu ◽  
Hanchao Yao ◽  
Hong Yang ◽  
...  

2019 ◽  
Vol 89 ◽  
pp. 102998 ◽  
Author(s):  
Ebru Taflan ◽  
Hacer Bayrak ◽  
Mehtap Er ◽  
Şengül Alpay Karaoğlu ◽  
Arif Bozdeveci

2014 ◽  
Vol 2 (11) ◽  
pp. 1557-1564 ◽  
Author(s):  
M. Vukomanović ◽  
M. Logar ◽  
S. D. Škapin ◽  
D. Suvorov

Structural analogy with antibacterial peptides provides antibacterial property in newly developed HAp/Au/arginine nanocomposite. The material possesses: (i) high antibacterial activity, (ii) high cytocompatibility and (iii) good stability in physiological environment.


2010 ◽  
Vol 76 (13) ◽  
pp. 4542-4545 ◽  
Author(s):  
Chih-Bo Hu ◽  
Wanna Malaphan ◽  
Takeshi Zendo ◽  
Jiro Nakayama ◽  
Kenji Sonomoto

ABSTRACT Enterocin X, composed of two antibacterial peptides (Xα and Xβ), is a novel class IIb bacteriocin from Enterococcus faecium KU-B5. When combined, Xα and Xβ display variably enhanced or reduced antibacterial activity toward a panel of indicators compared to each peptide individually. In E. faecium strains that produce enterocins A and B, such as KU-B5, only one additional bacteriocin had previously been known.


2018 ◽  
Author(s):  
Sajid Iqbal ◽  
Muhammad Qasim ◽  
Farida Begum ◽  
Hazir Rahman ◽  
Imran Sajid

AbstractAimsThe current study was designed to isolate, screen and identify the indigenous soil antibacterial exhibiting bacteria (AEB) and effect of various parameters on growth of AEB and antibacterial peptides production.Methods and resultsThe soil isolates were screened for antagonistic activity against a set of ATCC and local MDR human pathogenic bacterial strains. The antibacterial compound was protein in nature, exhibited no haemolysis and molecular weight was less than 20 KDa. The potential AEB isolate was identified by morphology, biochemical testing and by 16S rRNA gene sequencing asB. safensisMK-12. Growth and antibacterial activity was optimized forB. safensisstrain MK-12, exhibited maximum growth as well as antibacterial activity after 48 hours of incubation at pH 8, 30 °C in shaking incubator when fermented in optimized medium.ConclusionThe current study results indicate that indigenous soil is rich source of AEB and could be a promising source of antimicrobial compounds to fight against MDR bacteria in future.Significance and impactThis is the first scientific report on soil bacteria from northern region of Pakistan as per our knowledge. Therefore, screening of soil bacteria for antibacterial activity from unexplored area may contribute towards new antibiotic. Selected soil strain in the current study exhibited promising antibacterial activity against human pathogenic MDR bacterial strains.


2003 ◽  
Vol 70 (2) ◽  
pp. 189-197 ◽  
Author(s):  
Maria Baranyi ◽  
Ursula Thomas ◽  
Antonio Pellegrini

Acid-precipitated rabbit ‘whole casein’ was digested by trypsin, chymotrypsin, pepsin, and clostripain to screen for possible peptides with antibacterial properties. The peptide fragments were separated by reversed-phase chromatography. The collected fractions were pooled and their antibacterial properties tested against Escherichia coli, Bacillus subtilis and Staphylococcus lentus. Three antibacterial peptide fragments derived from tryptic digestion of rabbit casein were isolated and identified. Their sequences were found as follows: HVEQLLR (residues 50–56 of β-casein), ILPFIQSLFPFAER (residues 64–77 of β-casein), and FHLGHLK (residues 19–25 of αs1-casein). The three peptides were synthesized and found to exert antibacterial effect against Gram positive bacteria only. Proteolytic digestion of rabbit casein by chymotrypsin, pepsin and clostripain yielded several peptide fragments with antibacterial activity. Since antibiotic peptides can be released from casein during the digestion of milk proteins, our results suggest a possible antibacterial function of rabbit caseins. It is conceivable that antibacterial peptides can be generated by endopeptidases of the mammalian gastrointestinal tract possibly providing protection for new-born rabbits against aggression of micro-organisms.


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