The relationship between peptide structure and antibacterial activity.
نویسندگان
چکیده
Cationic antimicrobial peptides are a class of small, positively charged peptides known for their broad-spectrum antimicrobial activity. These peptides have also been shown to possess anti-viral and anti-cancer activity and, most recently, the ability to modulate the innate immune response. To date, a large number of antimicrobial peptides have been chemically characterized, however, few high-resolution structures are available. Structure-activity studies of these peptides reveal two main requirements for antimicrobial activity, (1) a cationic charge and (2) an induced amphipathic conformation. In addition to peptide conformation, the role of membrane lipid composition, specifically non-bilayer lipids, on peptide activity will also be discussed.
منابع مشابه
Purification and Characterization of an Antibacterial, Antifungal and Non Hemolytic Peptide from Rana Ridibunda
Amphibians have a large variety of antimicrobial peptides that serve as natural innate barriers limiting microbial infection or, in some instances, act as an integral component in response to inflammation or microbial infection. A novel peptide with antibacterial effects and without hemolytic activity was purified from skin secretions of Rana ridibunda by multisteps cation-exchange FPLC, revers...
متن کاملThree-dimensional quantitative structure activity relationship approach series of 3-Bromo-4-(1-H-3-Indolyl)-2, 5-Dihydro-1H-2, 5- Pyrroledione as antibacterial agents
The use of quantitative structure–activity relationships, since its advent, has becomeincreasingly helpful in understanding many aspects of biochemical interactions in drug research.This approach was utilized to explain the relationship of structure with biological activity ofantibacterial. For the development of new fungicides against, the quantitative structural–activityrelationship (QSAR) an...
متن کاملSynthesis of a peptide derivative of microcin J25 and evaluation of antibacterial and biological activities
Microcin J25 (MccJ25) is a small ribosomally synthesized antimicrobial peptide that is produced by Enterobacteriacea family especially E.coli. The present study focuses on preparation and evaluation of in vitro antimicrobial and biological properties of a new peptide derived from MccJ25. We prepared a MccJ25-derived peptide containing 14 amino acids and a single intra-molecular disulfide bond a...
متن کاملSynthesis of a peptide derivative of microcin J25 and evaluation of antibacterial and biological activities
Microcin J25 (MccJ25) is a small ribosomally synthesized antimicrobial peptide that is produced by Enterobacteriacea family especially E.coli. The present study focuses on preparation and evaluation of in vitro antimicrobial and biological properties of a new peptide derived from MccJ25. We prepared a MccJ25-derived peptide containing 14 amino acids and a single intra-molecular disulfide bond a...
متن کاملThe Identification of a Novel Peptide Derived from Lactoferrin Isolated from Camel Milk with Potential Antimicrobial Activity
Background and Objective: Antimicrobial peptides have attracted significant attention in recent decades because of their properties, such as rapid bactericidal effects, having a wide spectrum of activity, and a rare development of drug resistance. The purpose of this study was to examine the antibacterial activity of a peptide derived from the lactoferrin isolated from camel milk against Staphy...
متن کاملAntibacterial Activity of the Peptide Microcin J25 Produced by Escherichia coli
Background and objectives: Bacteriocins are generally active antimicrobial peptides effective against bacteria closely related to the producer. Escherichia coli produce two bacteriocins: colicins and microcins. Microcin J25 (Mcc J25) is an antibacterial peptide that inhibits bacterial transcription by disrupting the nucleotide-uptake channel of bacterial RNA polymerase. The objective of this st...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Peptides
دوره 24 11 شماره
صفحات -
تاریخ انتشار 2003