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Friday, March 23, 2018

CATHELICIDINS an antimicrobial peptide

Cathelicidins, a group of peptides having 100 amino acid domains that is habitually proteolytically divided from the exceedingly variable C-terminal antimicrobial domain. In phagocytes, the cathelicidins are usually put away as latent antecedents in secretory granules. Much of the time, the preparing protein is neutrophil elastase contained in a different arrangement of capacity granules. Amid phagocytosis, this twofold framework consolidates to create dynamic antimicrobial peptides. A wealth of evidence exists to suggest cathelicidin's crucial role as an antimicrobial in the protection of epithelial surfaces, particularly the skin. The clinical significance of cathelicidins antimicrobial activity can be seen in patients with Kostmann's syndrome, a rare genetic condition resulting in severe neutropenia. Cathelicidins are precursors of many novel peptides. Cathelicidin-derived antimicrobial peptides range in length from 12 to about 100 residues, and include α-helical peptides, e.g. human LL-37/hCAP18 and pig PMAP-37 ; linear peptides with one or two predominant amino acids, e.g. the bovine Pro- and Arg-rich Bac5 and Bac7  and the Trp-rich indolicidin ; and peptides with one or two disulfide bonds, e.g. bovine cyclic dodecapeptide  and pig protegrins The general lead of the component activating Cathelicidin activity, similar to that of other antimicrobial peptides, includes the breaking down (harming and puncturing) of cell layers of creatures toward which the peptide is dynamic. Cathelicidins don't follow up on solid host cell layer. Collaboration of cationic peptides and contrarily charged lipid films of microorganisms empower their precise, parallel bond and mooring, and killing the layer charge. Changing of the auxiliary and tertiary structure of the peptide changes its opposite introduction, in this way inserting in the lipid bilayer and making transmembrane pores. In its activity against Gram– negative microscopic organisms, the peptide can move over the external film, and in the wake of passing the layer of peptidoglycan, crosses the inward film into the cytoplasm of the bacterial cell. Cathelicidin has also proven to be effective against viral infections including herpes simplex virus, vaccinia virus, and fungal infections.

Wednesday, March 14, 2018

DEFENSINS An Antimicrobial Peptide

Defensins are small cysteinerich cationic proteins found in both vertebrates and invertebrates. They have also been reported in plants.  Also they are assorted individuals from a substantial group of cationic host Defense peptides (HDP), generally dispersed all through the plant and creature kingdoms. Defensins and Defensin-like peptides are practically different, disturbing microbial layers and going about as ligands for cellular recognition and signaling. They function as, host defense peptides. They are active against bacteria, fungi and many enveloped and non-enveloped viruses. They consist of 18-45 amino acids including six (in vertebrates) to eight conserved cysteine residues. These (Defensin) are especially plentiful and generally dispersed antimicrobial peptides described by a cationic β-sheet rich amphipathic structure balanced out by a preserved three-disulfide motif. They extend in measure from 29 to 47 amino acids, and are bottomless in numerous vertebrate granulocytes, Paneth cells (specific granule-rich intestinal host guard cells), and on epithelial surfaces. Like the more straightforward magainins and protegrins, defensins likewise shape pores in target films. There is confirming that the permeabilization of target cells is nonlethal unless taken after by Defensin passage into the cell and extra intracellular harm. AMP productions might be both constitutive and inducible. Defensin biosynthesis is specially activated by atomic structures related with pathogens of irresistible operators and furthermore by cytokines. Animals and human alpha and beta defensins separated in 1980th are additionally subdivided into various subtypes. There are numerous subtypes of alpha and beta defensins (e.g., αdef1; αdef3; αdef4; αdef6; βdef1; βdef2; βdef4, and so forth.); in multicellular living beings they assume comparable anti-infection parts against microorganisms, organisms, and even some infections The tadefensins (Θ) have been as of late found in a few individuals from the set of all animals. These antibacterial peptides go about as commit porins on the bacterial cell divider. Not at all like the insects and mammalian defensins, are which for the most part dynamic against bacteria. Plant defensins, with a couple of exemptions, don't have antibacterial movement. Most plant defensins are engaged with resistance against an expansive scope of organisms.  They are not just dynamic against phytopathogenic growths, (for example, Fusarium culmorum and Botrytis cinerea), yet additionally against cook's yeast and human pathogenic organisms, (for example, Candida albicans. Plant defensins have likewise been appeared to hinder the development of roots and root hairs in Arabidopsis thaliana and change development of different tomato organs which can expect numerous capacities identified with safeguard and advancement. 

Monday, March 12, 2018

MALACIDINS a new class of antibiotics

Researchers from The Rockefeller University have discovered a new class of antibiotics capable of killing off several antibiotic-resistant pathogens. This new family comes from molecules present in a large variety of soils and researchers hope it could be a useful weapon in our medical arsenal.
As reported in Nature Microbiology, the antibiotic compounds are a special class of peptides – special chains of amino acids – which require calcium for antibacterial activity. Calcium-dependent antibiotics are capable of targeting bacteria in a variety of ways and this characteristic makes them particularly effective. They can target the formation of the bacterial cell membrane or even destroy the cell wall.
The team looked for new members of this antibiotic family and tested them against known pathogens. The new antibiotics, called malacidins, were successful in sterilizing methicillin-resistant Staphylococcus aureus, also known as the superbug MRSA, and the bacteria attacked with the malacidins did not develop resistance.

The new family of antibiotics comes from molecules present in large variety of soils. Scientists had analysed more than 1000 unique soil samples across US to better understand how new class of antibiotics is produced and how it can be exploited for fighting bacteria. They had used DNA information that encodes production of antibiotic in daptomycin to study it. This discovery could be a useful weapon in field of medicines.

Significance

Malacidins are distinctive class of antibiotics that are commonly encoded in soil microbiomes. They have never been reported in culture-based NP (Natural Products) discovery efforts.
Malacidins are active against multidrug-resistant pathogens, sterilise methicillin-resistant Staphylococcus aureus  (MRSA) skin infections in animal wound model and did not select for resistance in laboratory conditions.
The malacidins was tested on rats with MRSA skin infections. The condition was cured, and even after 20 days of continued contact with malacidins, the rodents did not experience any side effects.

Concern

Malacidins only target gram-positive bacteria with a very thick cell wall. It is ineffective against gram-negative bacteria which cause cholera, pneumonia, sexually transmitted diseases, and plague. Thus, it does not make it universal cure against all bacteria.

Saturday, March 10, 2018

Facts about Our Digestive system

 • We eat about 500kg of food per year.
1.7 liters of saliva is produced each day.
The esophagus is approximately 25cm long.
Muscles contract in waves to move the food down the esophagus. This means that food would get to a person's stomach, even if they were standing on their head.
An adult's stomach can hold approximately 1.5 liters of material.
Every day 11.5 liters of digested food, liquids and digestive juices flow through the digestive system, but only 100 mls is lost in feces.
In the mouth, food is either cooled or warmed to a more suitable temperature.
Our digestive system has its own little mini-brain.                       
     The functioning of the digestive system is regulated by the enteric nervous system (ENS), which is made up of a tremendous amount of nerve cells and is regulated by the same neurotransmitters, most notably serotonin, found in the brain. This similarity has earned the ENS the title of the "Second Brain".our brain and digestive system work in close partnership, a phenomenon that we have first-hand knowledge of any time our stomach flips when we think of something anxiety-provoking — or more dramatically if we experience diarrhea when we are stressed. This collaboration is thought to be essential to our survival as a species; although digestion is essential for life, dealing with threats is just as necessary. The body developed the "flight or fight" system to divert resources away from the digestive system to the systems of the body needed to fight off or run away from things that might do us harm. Dysfunction in the brain-gut connection has been theorized to play a role in the development of functional gastrointestinal disorders (FGDs).

Wednesday, March 07, 2018

Application of Histatin 5 Derivative, Defensin and Cathelicidin Peptides as Antimicrobial Agents (Amps)

Sunday, March 04, 2018

Microbial Resistance Mechanism from Peptides

Protection from AMPs by a touchy strain of microorganism is improbable due to their incredible decent variety and the way that they have been powerful against bacterial contaminations for no less than 108 years. In any case, a few pathogens are more impervious to AMPs and others are more touchy. For instance, safe types of such sorts as Serratia and Morganella have an external layer lacking the proper thickness of the acidic lipids which are peptide restricting destinations. Other safe species, for example, Porphyromonas gingivalis discharge stomach related proteases that annihilate the peptide. Cationic antimicrobial peptides (CAMPs) are fundamental mixes of the antimicrobial weapons stores in practically a wide range of life forms, with imperative parts in microbial nature and higher organism's host defense. Numerous microscopic organisms have created countermeasures to constrain the viability of CAMPs, for example, defensins, Cathelicidins, kinocidins, or bacteriocins. The best-considered bacterial CAMP protection components include electrostatic repulsions of CAMPs by change of cell envelope particles, proteolytic cleavage of CAMPs, creation of CAMP-catching proteins, or expulsion of CAMPs by vitality subordinate efflux pumps. The collection of CAMPs created by a given host living being and the productivity of microbial CAMP protection components seem, by all accounts, to be significant in have pathogen cooperation’s, administering the structure of commensal microbial groups and the destructiveness of bacterial pathogens. Be that as it may, all CAMP protection instruments have constraints and microbes have never prevailing with regards to ending up completely inhumane to a wide scope of CAMPs. CAMPs or preserved CAMP protection factors are talked about as new middle people and targets, individually, of novel and supportable hostile to infective systems. 

Friday, March 02, 2018

MECHANISM AND ACTION OF ANTIPEPTIDES

Mechanism of Peptides Derivatives Anti peptides or proteins are the inhibitory factors or proteins which are being designed to inhibit the function of defective ones. A striking component among antimicrobial peptides as a gathering is their general preservation of structure and charge topics crosswise over assorted phyla. Regardless of whether combined non-ribosomal with d-and l-amino acids, or from hereditarily encoded messenger RNA, antimicrobial peptides frame amphipathic structures and are frequently cationic at physiological pH. The amphipathicity and net charge are qualities justifiably moderated among numerous antimicrobial peptides. Besides, charge liking is likely an imperative means presenting selectivity to antimicrobial peptides. With regards to these ideal models, the accompanying exchange features momentum ideas identifying with the atomic premise of antimicrobial peptide systems of activity. AMP's Kill cells by upsetting layer respectability (through communication with Negatively charged cell membrane ), by repressing proteins, DNA and RNA union, or by collaborating with certain intracellular targets.   
Be that as it may, the idea that AMPs should be cationic was changed later with the disclosure of adversely charged AMPs in 1997. For instance maximin-H5 from frog skin and dermicidin discharged from sweat organ tissues of human are both anionic peptides. By and large an AMP is just successful against one class of microorganisms (e.g., microbes or growths). Notwithstanding, there are special cases and a few AMPs are known to have diverse methods of activity against diverse sorts of microorganisms.  For instance, indolicidin can eliminate microscopic organisms, parasites, and HIV. They also displays antifungal18 exercises by making harms cell film. Be that as it may, it slaughters E. coli by entering into the phones and hindering DNA amalgamation; and it demonstrates against HIV exercises by restraining HIV-integrase. In correlation; a few AMPs have a similar method of murdering of various cell sorts. For instance, PMAP-23 can execute the two growths and parasites by framing pores in their cell layers. A fundamental necessity for any antimicrobial host safeguard or restorative operator is that it has a specific poisonous quality for the microbial target with respect to the host. In a perfect world, such mixes have fondness for at least one microbial determinant that is effortlessly open, regular to a wide range of organisms, and moderately changeless. Nature has evidently yielded a class of particles that meets these imperatives in the development of antimicrobial peptides. Antimicrobial peptides at first target microbial cells, and consequently satisfy criteria plot above for distinguishing sub-atomic determinants of pathogens that are open and comprehensively saved. 

Thursday, March 01, 2018

Antimicrobial Peptide

Peptides (proteins) that are basically hydrophobic and hydrophilic and predominately either anionic or cationic are regularly found to be able to kill organisms or potentially cancer cells. There are an expansive scope of antimicrobial peptides (AMPs) that have been distinguished from an assortment of life forms have been found to slaughter organisms as well as execute cancer cells. Subsequently numerous AMPs are or conceivably are anticancer peptides (ACPs) .The rapid increase in drug-resistant infections has presented a serious challenge to antimicrobial and anticancer therapies. The capability of peptides in Cancer and microbial treatment is obvious from a wide range of techniques that are accessible to address the movement of tumor and disease development and proliferation of the infection. Utilization of peptides that can specifically target inadequate cells without influencing typical cells (directed treatment or targeted treatment) is advancing as a substitute system to regular chemotherapy. Peptide can be used straightforwardly as a cytotoxic operator through different systems or can go about as a bearer of cytotoxic specialists and radioisotopes by particularly focusing on disease cells. Peptide-based hormonal treatment has been broadly contemplated and used for the treatment of breast and prostate diseases. Gigantic measure of clinical information is as of now accessible authenticating the productivity of peptide-based growth and microbial immunizations. The failure of the most potent antibiotics to kill “superbugs” emphasizes the urgent need to develop other control agents.
Antimicrobial peptides (AMPs) are oligopeptides with a varying number (from five to over a hundred) of amino acids. Antimicrobial peptides (AMPs) are small sub-atomic weight proteins with broad spectrum   antimicrobial action against microscopic organisms like viruses, fungi, and parasites. These developmentally moderated peptides are generally positively charged and have both a hydrophobic and hydrophilic side that empowers the particle to be dissolvable in watery conditions yet likewise enter lipid-rich layers .Once in an objective microbial layer, the peptide kills target cells through differing components. Cathelicidins and defensins are real gatherings of epidermal AMPs. Diminished levels of these peptides have been noted for patients with atopic dermatitis and Kostmann's disorder, an innate neutropenia. Notwithstanding essential antimicrobial properties, developing confirmation demonstrates that AMPs modify the host invulnerable reaction through receptor-subordinate cooperation’s. AMPs have been appeared to be critical in such various capacities as angiogenesis, wound mending, and chemotaxis. As part of our research programme for development of  biologically active compounds here we are discussing the action and mechanism of the antimicrobial activities of peptides.