نتایج جستجو برای: antimicrobial peptides

تعداد نتایج: 158971  

Journal: :Biomacromolecules 2008
D Matthew Eby Karen E Farrington Glenn R Johnson

Amphiphilicity and cationicity are properties shared between antimicrobial peptides and proteins that catalyze biomineralization reactions. Merging these two functionalities, we demonstrate a reaction where a cationic antimicrobial peptide catalyzes self-biomineralization within inorganic matrices. The resultant antimicrobial peptide nanoparticles retain biocidal activity, protect the peptide f...

Journal: :Molecular simulation 2009
Abdallah Sayyed-Ahmad Himanshu Khandelia Yiannis N Kaznessis

We present relative binding free energy calculations for six antimicrobial peptide-micelle systems, three peptides interacting with two types of micelles. The peptides are the scorpion derived antimicrobial peptide (AMP), IsCT and two of its analogues. The micelles are dodecylphosphatidylcholine (DPC) and sodium dodecylsulphate (SDS) micelles. The interfacial electrostatic properties of DPC and...

Fatemeh Elmi, Hassan Hoda, Maryam Mytra Elmi,

ABSTRACT Background Antibiotic resistance makes antimicrobial peptides (AMPs) agents an alternative for treatment of pathogenic diseases. They are isolated from various animals invertebrates, vertebrates and plants. The present study shows the electrophoretic pattern of protein and peptides from Vicia Faba seed and reports our first attempt to study the antibacterial activity of Vicia faba...

Journal: :The Journal of nutrition 2005
Shruti M Phadke Berthony Deslouches Sara E Hileman Ronald C Montelaro Harold C Wiesenfeld Timothy A Mietzner

The antimicrobial activity of the collective molecules comprising human milk reflects an evolutionarily successful paradigm for preventing and limiting microbial infection. Understanding the molecules that participate in this process and how they work can yield insight into potentially new antimicrobial therapies. Upon proteolytic processing, antimicrobial peptides can be derived from milk prot...

Journal: :Biochimica et biophysica acta 2006
Suzana K Straus Robert E W Hancock

With the steady rise in the number of antibiotic-resistant Gram-positive pathogens, it has become increasingly important to find new antibacterial agents which are highly active and have novel and diversified mechanisms of action. Two classes will be discussed here: the cationic antimicrobial peptides, which are amphiphilic in nature, targeting membranes and increasing their permeability; and l...

Abstract Background and purpose: Multiple drug-resistant (MDR) bacterial strains have spread in different parts of hospitals. The aim of this study was to design and synthesize an effective hybrid peptide by combining different parts of two peptides to achieve the highest antibacterial activity and its inhibitory effect against Staphylococcus aureus and Pseudomonas aeruginosa strains. Materia...

Journal: :Clinical microbiology reviews 2006
Håvard Jenssen Pamela Hamill Robert E W Hancock

Antimicrobial host defense peptides are produced by all complex organisms as well as some microbes and have diverse and complex antimicrobial activities. Collectively these peptides demonstrate a broad range of antiviral and antibacterial activities and modes of action, and it is important to distinguish between direct microbicidal and indirect activities against such pathogens. The structural ...

Journal: :Chemical Science 2021

Machine learning models trained with experimental data for antimicrobial activity and hemolysis are shown to produce new non-hemolytic peptides active against multidrug-resistant bacteria.

2014
Jorge A. Masso-Silva Gill Diamond

Antimicrobial peptides (AMPs) are found widely distributed through Nature, and participate in the innate host defense of each species. Fish are a great source of these peptides, as they express all of the major classes of AMPs, including defensins, cathelicidins, hepcidins, histone-derived peptides, and a fish-specific class of the cecropin family, called piscidins. As with other species, the f...

2017
L. L. Greiner T. S. Stahly T. Stanton

The objectives of this research were to validate the sensitivity and precision of an in vitro assay for evaluating the efficacy of antimicrobials, to evaluate the ability of natural animal proteins/peptides to kill in vitro antibiotic-resistant, as well as, -susceptible bacteria, and to determine the effects of key components of animal digesta (e.g., pH, mineral content, and proteolytic digesti...

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