Cationic Antibacterial Peptides Research Articles

Exploring novel peptides in adzuki bean and mung bean hydrolysates with potent antibacterial activity

SummaryThis study delved into the antimicrobial potential of hydrolysates from adzuki bean and mung bean protein concentrates, created using Alcalase and Flavourzyme enzymes. Targeting common foodborne pathogens (Salmonella Typhimurium, Salmonella Enteritidis, Vibrio parahaemolyticus, Staphylococcus aureus, and Bacillus subtilis) and Escherichia coli, the research underscored the crucial role of peptidase in generating antibacterial peptides. Fractions F2 of Flavourzyme hydrolysed adzuki bean (ABF) and F4 of Flavourzyme hydrolysed mung bean (MBF) showed the highest antibacterial activity against S. Typhimurium and S. aureus, respectively, whereas F2 of Alcalase hydrolysed mung bean (MBA) exhibited very poor activity against S. aureus. TripleTOF LC–MS/MS analysis revealed small cationic antibacterial peptides, with lysine being prominent against S. aureus and proline–proline against S. Typhimurium. These findings highlighted the significant contribution of protease enzymes in fostering antibacterial peptide production, offering valuable insights for developing effective antimicrobial agents in the context of food safety.

Progress in the design principle of biomedical tissue adhesive hydrogel with naturally derived substance

AbstractIn recent years, natural substance‐based tissue adhesive hydrogels have been widely studied by researchers because of their practicability and affordability. In this review, we summarized the design principles and mechanisms for constructing natural substance‐based tissue adhesive hydrogels from the perspective of polyphenols (catechol, dopamine, tannic acid), cationic polymers (chitosan, lysine, cationic antibacterial peptides), polysaccharides and other natural substances. In addition, according to the morphology and size of tissue adhesive hydrogels, it was divided into macroscopic hydrogels and microscopic hydrogels. Therefore, the natural substance‐based adhesive macroscopic hydrogels such as injectable hydrogels and hydrogel patches and natural substance‐based adhesive microscopic hydrogels including hydrogel microspheres were reviewed. Furthermore, we summarized the review and provided outlook based on the present tissue adhesive hydrogels. The review aimed to summarize the progress in natural substance‐based tissue adhesive hydrogels and provide a valuable reference for the development of tissue adhesive hydrogels and its applications in biomedical field.

Development of cannabidiol derivatives as potent broad-spectrum antibacterial agents with membrane-disruptive mechanism

The emergence of antibiotic resistance has brought a significant burden to public health. Here, we designed and synthesized a series of cannabidiol derivatives by biomimicking the structure and function of cationic antibacterial peptides. This is the first report on the design of cannabidiol derivatives as broad-spectrum antibacterial agents. Through the structure-activity relationship (SAR) study, we found a lead compound 23 that killed both Gram-negative and Gram-positive bacteria via a membrane-targeting mechanism of action with low resistance frequencies. Compound 23 also exhibited very weak hemolytic activity, low toxicity toward mammalian cells, and rapid bactericidal properties. To further validate the membrane action mechanism of compound 23, we performed transcriptomic analysis using RNA-seq, which revealed that treatment with compound 23 altered many cell wall/membrane/envelope biogenesis-related genes in Gram-positive and Gram-negative bacteria. More importantly, compound 23 showed potent in vivo antibacterial efficacy in murine corneal infection models caused by Staphylococcus aureus or Pseudomonas aeruginosa. These findings would provide a new design idea for the discovery of novel broad-spectrum antibacterial agents to overcome the antibiotic resistance crisis.

Antibacterial activity of active peptide from marine macroalgae Chondrus crispus protein hydrolysate against Staphylococcus aureus

Macroalgae is a protein source with the potential to yield antimicrobial peptides (AMPs) that exhibit a wide range of biological activities. This study aimed to find bioactive peptide-based antibacterial compounds from marine macroalgae Chondrus crispus protein hydrolysate. The peptides were isolated by solid phase extraction with a strong cation exchanger from trypsin-digested and α-chymotrypsin-digested hydrolysates. Certain fractions of the hydrolyzed protein displayed a good inhibition zone, with the α-chymotrypsin-digested fraction eluted at pH 9 exhibiting the highest inhibition against Gram-negative bacteria Staphylococcus aureus. Several peptides were characterized as cationic helical peptides with hydrophobicity percentages of 16.67–77.78%. The potential antibacterial peptide P01 KKNVTTLAPLVF was identified as an α-helical cationic antibacterial peptide with 0.525 GRAVY value, amphipathic structure, and +2 total charge. Moreover, strong interaction was observed between P07 SAGSGNEGLSGW and P20 RTASSR peptide with DNA gyrase and DHFR receptors from S. aureus with binding energy -8.0 and -7.3 kcal/mol, respectively.

Membrane-Active Nonivamide Derivatives as Effective Broad-Spectrum Antimicrobials: Rational Design, Synthesis, and Biological Evaluation.

Antibiotic resistance is emerging as a "global public health concern". To address the growing epidemic of multidrug-resistant pathogens, the development of novel antimicrobials is urgently needed. In this study, by biomimicking cationic antibacterial peptides, we designed and synthesized a series of new membrane-active nonivamide and capsaicin derivatives as peptidomimetic antimicrobials. Through modulating charge/hydrophobicity balance and rationalizing structure-activity relationships of these peptidomimetics, compound 51 was identified as the lead compound. Compound 51 exhibited potent antibacterial activity against both Gram-positive bacteria (MICs = 0.39-0.78 μg/mL) and Gram-negative bacteria (MICs = 1.56-6.25 μg/mL), with low hemolytic activity and low cytotoxicity. Compound 51 displayed a faster bactericidal action through a membrane-disruptive mechanism and avoided bacterial resistance development. Furthermore, compound 51 significantly reduced the microbial burden in a murine model of keratitis infected by Staphylococcus aureus or Pseudomonas aeruginosa. Hence, this design strategy can provide a promising and effective solution to overcome antibiotic resistance.

Membrane Disruptive Action of Cationic Antibacterial Peptide B1CTcu3.

A twenty-two-residue peptide Brevinin1 Clinotarsus curtipus-3 (B1CTcu3), identified from the skin secretion of frog Clinotarsus curtipes of the Western Ghats, exhibited a broad range of antibacterial activity against Gram-negative and Gram-positive bacteria, including the methicillin-resistant Staphylococcus aureus (MRSA). It showed anti-biofilm activity even at sub-minimum inhibitory concentration (sub-MIC) against Pseudomonas aeruginosa and Staphylococcus aureus. Analysis of the scanning electron microscopic (SEM) images, confocal images, flow cytometric data and the effect of salt concentration on antibacterial potency suggests that the killing action of the peptide is through the membranolytic process. Single channel electric recording confirmed that the peptide elicited pores on the bacterial cell membrane as it induces a heterogeneous channel in the lipid bilayer. It also showed cytotoxicity against MDA-MB-231 breast cancer cell with IC50 of 25 μM. B1CTcu3 peptide could serve as the template for next-generation antibacterial agents, particularly against antibiotic resistant pathogenic bacteria.

LL-37 transports immunoreactive cGAMP to activate STING signaling and enhance interferon-mediated host antiviral immunity.

Cyclic 2',3'-GMP-AMP (cGAMP) binds to and activates stimulator of interferon genes (STING), which then induces interferons to drive immune responses against tumors and pathogens. Exogenous cGAMP produced by infected and malignant cells and synthetic cGAMP used in immunotherapy must traverse the cell membrane to activate STING in target cells. However, as an anionic hydrophilic molecule, cGAMP is not inherently membrane permeable. Here, we show that LL-37, a human host defense peptide, can function as a transporter of cGAMP. LL-37 specifically binds cGAMP and efficiently delivers cGAMP into target cells. cGAMP transferred by LL-37 activates robust interferon responses and host antiviral immunity in a STING-dependent manner. Furthermore, we report that LL-37 inducers vitamin D3 and sodium butyrate promote host immunity by enhancing endogenous LL-37 expression and its mediated cGAMP immune response. Collectively, our data uncover an essential role of LL-37 in innate immune activation and suggest new strategies for immunotherapy.

New short cationic antibacterial peptides. Synthesis, biological activity and mechanism of action

We report a theoretical and experimental study on a new series of small-sized antibacterial peptides. Synthesis and bioassays for these peptides are reported here. In addition, we evaluated different physicochemical parameters that modulate antimicrobial activity (charge, secondary structure, amphipathicity, hydrophobicity and polarity). We also performed molecular dynamic simulations to assess the interaction between these peptides and their molecular target (the membrane). Biophysical characterization of the peptides was carried out with different techniques, such as circular dichroism (CD), linear dichroism (LD), infrared spectroscopy (IR), dynamic light scattering (DLS), fluorescence spectroscopy and TEM studies using model systems (liposomes) for mammalian and bacterial membranes. The results of this study allow us to draw important conclusions on three different aspects. Theoretical and experimental results indicate that small-sized peptides have a particular mechanism of action that is different to that of large peptides. These results provide additional support for a previously proposed four-step mechanism of action. The possible pharmacophoric requirement for these small-sized peptides is discussed. Furthermore, our results indicate that a net +4 charge is the adequate for 9 amino acid long peptides to produce antibacterial activity. The information reported here is very important for designing new antibacterial peptides with these structural characteristics.

Design, Synthesis, and Biological Evaluation of Membrane-Active Bakuchiol Derivatives as Effective Broad-Spectrum Antibacterial Agents

Infections caused by drug-resistant bacteria seriously endanger human health and global public health. Therefore, it is urgent to discover and develop novel antimicrobial agents to combat multidrug-resistant bacteria. In this study, we designed and synthesized a series of new membrane-active bakuchiol derivatives by biomimicking the structure and function of cationic antibacterial peptides. The most promising compound 28 displayed potent antibacterial activity against both Gram-positive bacteria (minimum inhibitory concentration, MIC = 1.56-3.125 μg/mL) and Gram-negative bacteria (MIC = 3.125 μg/mL), very weak hemolytic activity, and low cytotoxicity. Compound 28 had rapid bactericidal properties and avoided bacterial resistance. More importantly, compound 28 showed strong in vivo antibacterial efficacy against Staphylococcus aureus and Pseudomonas aeruginosa in murine corneal infection models. This design strategy is expected to provide an effective solution to the antibiotic crisis.

Impact of Polymyxin Resistance on Virulence and Fitness among Clinically Important Gram-Negative Bacteria

Humanity is facing an enormous and growing worldwide threat from the emergence of multi-drug-resistant (MDR) Gram-negative bacteria such as Escherichia coli , Klebsiella pneumoniae , and Acinetobacter baumannii . Polymyxin B and E (colistin) constitute the last-line therapies for treating MDR Gram-negative bacteria. Polymyxin is a cationic antibacterial peptide that can destroy the outer membrane of Gram-negative bacteria. With the increasing clinical application of polymyxin, however, there have been many reports of the occurrence of polymyxin-resistant Gram-negative bacteria. This resistance is mainly mediated by the modification or complete loss of lipopolysaccharide (LPS). LPS is also a virulence factor of Gram-negative bacteria, and alterations of LPS may correlate with virulence. Although it is generally believed that the biological costs associated with drug resistance may enable benign susceptible bacteria to overcome resistant bacteria when antibiotic pressure is reduced, some studies have shown that polymyxin-resistant bacteria are associated with higher virulence and greater fitness compared with their susceptible counterparts. To predict the development of polymyxin resistance and evaluate interventions for its mitigation, it is important to understand the relative biological cost of polymyxin resistance compared with susceptibility. The impact of polymyxin resistance mechanisms on the virulence and fitness of these three Gram-negative bacteria are summarized in this review.

Морфологическая характеристика экспериментальной катетер-ассоциированной инфекции на фоне иммуносупрессии и применения низкомолекулярного катионного пептида семейства лантибиотиков – варнерина

Introduction. Catheter-associated infection is caused by microorganism colonization of the surface of the implanted catheter with a biofilm formation that significantly increases their resistance to antiseptics and antibiotics, especially in immunosuppression. Low-molecular antibacterial peptides are compounds capable of combating biofilm formation. The aim of the study was to describe morphological characteristics of a catheter-associated infection model on laboratory mice secondary to immunosuppression and to assess the efficacy of the low-molecular cationic antibacterial peptide (warnerin). Materials and methods. An experiment included white outbred mice (25–30 g body weight) under ether anesthesia that received 1.0-cm fragments of intravascular catheters under the skin of the backs. The animals underwent preliminary immunosuppression with cyclophosphamide. We used Staphylococcus epidermidis 33 (in the form of suspensions or biofilms previously grown on catheter segments) and low-molecular cationic peptide warnerin. All animals were sacrificed by ether overdose on days 1, 2, and 3 after the manipulation. We took the tissues surrounding the catheter for histological and immunohistochemical studies with antibodies to CD34, vimentin, CD68, CD3, and CD20. Results. The warnerin administration at the site of the catheter implantation led to disappearance of or a significant decrease in the number of bacterial. In the infiltrate, the number of neutrophils significantly increased, whereas that of fibroblasts decreased. Immunohistochemistry confirmed the features of the cellular reactions around the catheters with bacterial contamination with warnerin administration. Conclusion. In a model of catheter-associated infection in immunosuppressed mice, the warnerin antibacterial manifests in characteristic histological alterations in the inflammatory infiltrate composition. Keywords: catheter-associated infection model, morphology of inflammation, warnerin antibacterial cationic peptide

Molecular and functional identification of a β-defensin homolog in large yellow croaker (Larimichthys crocea).

β-defensin (BD) is a cysteine-rich cationic antibacterial peptide that is active against a wide range of bacteria. Here, a β-defensin homolog (LcBD2) was identified in large yellow croaker (Larimichthys crocea). The open reading frame of LcBD2 contains 195 nucleotides, encoding a protein of 64 amino acids that possesses a typical arrangement of six conserved cysteine residues (C31 , C37 , C41 , C53 , C59 and C60 ). LcBD2 transcripts were constitutively expressed in all examined tissues and significantly increased in head kidney, spleen and gills by Vibrio alginolyticus. The synthetic LcBD2 peptide imparted antimicrobial effects on both Gram-negative bacteria (V. campbellii, V. parahaemolyticus, V. alginolyticus, V. harveyi and Pseudomonas plecoglossicida) and Gram-positive bacteria (Bacillus subtilis). We also observed that after treatment with synthetic LcBD2 peptide, numerous blisters appeared on the membrane of P. plecoglossicida, which in turn may result in cell membrane breakage and bacterial death. Moreover, the synthetic LcBD2 peptide significantly upregulated the expression levels of TNF-α2, IL-1β and CXCL8_L1 in monocytes/macrophages, while downregulated expression level of IL-10. The LcBD2 peptide also remarkedly enhanced the phagocytosis of monocytes/macrophages. These results indicate that LcBD2 not only protects large yellow croaker against multiple bacterial pathogens but also plays a role in activation of monocytes/macrophages.

Antimicrobial and antitumor activity of peptidomimetics synthesized from amino acids

Thirteen cationic peptidomimetics derived from amino acids bearing an alkyl or ethynylphenyl moiety that mimic the structure of cationic antibacterial peptides were designed and synthesized using a simple coupling reaction of an amino acid with a substituted amine. Antibacterial activities of the resulting peptidomimetics against drug-sensitive bacteria, such as Gram-positive Staphylococcus aureus (S. aureus) and Bacillus subtilis, Gram-negative Escherichia coli (E. coli) and Salmonella enterica, and a drug-resistant bacterium, methicillin-resistant S. aureus (MRSA), were systematically evaluated. Most peptidomimetics show significant broad-spectrum antibacterial activity. A-L-Iso-C12 (isoleucine derivative bearing a dodecyl moiety) show MICs of 2.5 μg/mL against S. aureus and 4 μg/mL against MRSA and A-L-Val-C12 (valine derivative bearing a dodecyl moiety) show MICs of 1.67 μg/mL against E. coli and 8.3 μg/mL against MRSA. A-L-Val-C12 showed low cytotoxicity toward L929 cells in comparison with SGC 7901 cells, indicating tumor-directed killing by peptidomimetics while avoiding toxicity to normal cells. The influences of type of amino acid and substituent, length of substituent, and stereochemistry of amino acids on antibacterial activity and cytotoxicity of peptidomimetics were systematically investigated. The results indicate that this series of cationic peptidomimetics derived from amino acids display antitumor activity and may be useful for treatment of bacterial infections.

Preparation, Characterization and Pharmacokinetic Study of N-Terminal PEGylated D-Form Antimicrobial Peptide OM19r-8.

Recently, new cationic antibacterial peptide OM19R has been designed with low minimum inhibitory concentration (MIC) values against some gram-negative bacteria, such as Escherichia coli, Salmonella, and Shigella. However, this hybrid peptide, like most antibacterial peptides, has low enzyme stability and short half-life, which, in turn, increases the drug's cost. In this study, an antibacterial peptide (OM19r-8) was obtained containing some D-Arg amino acids. The new preparations were carried out through the replacement of l-Arginine by d-Arginine and the addition of PEG chains. Firstly, eight OM19r series of antibacterial peptides were obtained by designing D-Arg. Then, a polyethylene glycol-modified product mPEG5-butyrALD-OM19r-8 (mPEG5-OM19r-8) was isolated and purified by reverse-phase high-performance liquid chromatography (RT-HPLC). The enzyme stability test showed that the resistance of antibacterial peptide OM19r-8 to protease degradation increased by 4-32-fold. Moreover, the Time-kill studies showed that the germicidal kinetics curves of mPEG5-OM19r-8 and OM19r-8 to Escherichia coli had a similar trend, thus suggesting that PEG modification has an acceptable effect on the activity of the original peptide. Furthermore, the elimination of half-life (28.09±2.81min) of mPEG5-OM19r-8, and the area under the drug concentration-time curve (2686.48±651.36min∗ug/ml) was significantly prolonged. The current study demonstrates an example that optimizes the AMP by utilizing L-to-D amino acid replacement and including PEG chains. These results provide useful data for the clinical application of the mPEG5-OM19r-8.

SppI Forms a Membrane Protein Complex with SppA and Inhibits Its Protease Activity in Bacillus subtilis.

The membrane protease SppA of Bacillus subtilis was first described as a signal peptide peptidase and later shown to confer resistance to lantibiotics. Here, we report that SppA forms octameric complexes with YteJ, a membrane protein of thus-far-unknown function. Interestingly, sppA and yteJ deletion mutants exhibited no protein secretion defects. However, these mutant strains differed significantly in their resistance to antimicrobial peptides. In particular, sppA mutant cells displayed increased sensitivity to the lantibiotics nisin and subtilin and the human lysozyme-derived cationic antimicrobial peptide LP9. Importantly, YteJ was shown to antagonize SppA activity both in vivo and in vitro, and this SppA-inhibitory activity involved the C-terminal domain of YteJ, which was therefore renamed SppI. Most likely, SppI-mediated control is needed to protect B. subtilis against the potentially detrimental protease activity of SppA since a mutant overexpressing sppA by itself displayed defects in cell division. Altogether, we conclude that the SppA-SppI complex of B. subtilis has a major role in protection against antimicrobial peptides.IMPORTANCE Our study presents new insights into the molecular mechanism that regulates the activity of SppA, a widely conserved bacterial membrane protease. We show that the membrane proteins SppA and SppI form a complex in the Gram-positive model bacterium B. subtilis and that SppI inhibits SppA protease activity in vitro and in vivo Furthermore, we demonstrate that the C-terminal domain of SppI is involved in SppA inhibition. Since SppA, through its protease activity, contributes directly to resistance to lantibiotic peptides and cationic antibacterial peptides, we propose that the conserved SppA-SppI complex could play a major role in the evasion of bactericidal peptides, including those produced as part of human innate immune defenses.

B1CTcu5: A frog-derived brevinin-1 peptide with anti-tuberculosis activity

Tuberculosis (TB) is a devastating infectious disease that causes a high rate of mortality. Drugs with new modes of action are needed to overcome this scenario. Cationic antibacterial peptides can serve as a potential alternative to existing TB drugs as they target the entire bacterial membrane for activity, thereby reducing the probability of development of drug resistance. In this study, we report anti-tuberculosis activity of B1CTcu5, a peptide that belongs to brevinin-1 family of antimicrobial peptides. This peptide possesses potent in vitro inhibitory activity against M. tuberculosis at 12.5 μg/mL but was not active against M. smegmatis. B1CTcu5 successfully eliminated intracellular mycobacteria without inducing cytotoxicity to the human macrophages at the concentrations tested. This peptide can be used as a template to design peptide-based anti-tubercular agents.

A Dual Drug Delivery Platform for Cancer-Bacteria Cotargeting.

Bacteria can associate with mammalian cells in different ways. While some are essential for the body, others can manipulate their local environment to cause tumor-like conditions or find refuge in already existing cancerous tissues or cells, impacting not only chemotherapy through drug transformation but also antibiotic resistance through immune evasion. Despite these facts, cancer and bacterial therapies continue to be administered independently. We have developed a dual drug delivery platform, called "dualosome", that not only targets cancer cells but also clears bacteria from the cancer niche. Dualosomes comprise liposomes loaded with an anticancer drug (doxorubicin) in their core and a cationic antibacterial peptide (sushi S3) on their surface. Folic acid is also attached to the liposomal surface to impart cancer cell specificity. The efficacy of dualosomes is demonstrated on model S. typhi-infected hepatoma (Huh-7) cells, and it shows that the copackaged system is at least 75% more effective in eliminating both cell types than either drug alone, in the nanoformulated or free form. This improved performance is attributed to the bacteria-linked doxorubicin activity, as well as the enhanced internalization of the liposomes due to their cationic surface charge. Overall, our system holds great promise for curbing cancer-related bacterial infections and drug resistance in both cell types.

Recombinant porcine NK-lysin inhibits the invasion of hepatocellular carcinoma cells in vitro

The therapeutics having ability to target cancer cells specifically and exhibit nominal cytopathic effect on normal healthy cells are highly significant for cancer therapeutic applications. Recombinant porcine natural killer lysin (rpNK-lysin) has proven cationic anti-bacterial and anti-tumor peptide. Herein, we report its anti-invasion and anti-metastasis effects on hepatocellular carcinoma (HCC) cells in vitro. We first investigate the maximum non-toxic concentration (MNTC) of rpNK-lysin for the normal hepato cells (L-02). Using MNTC rpNK-lysin, we explore anti-proliferative, anti-adhesive, anti-invasive and anti-metastatic effect of rpNK-lysin on three different HCC cells lines (SMMC-7721, 97-H and HepG2) through MTT, wound-healing, adhesion and invasion assay along with mRNA and protein expression. The results reveal that rpNK-lysin has potential to specifically inhibit HCC cells growth in a dose and time-dependent manner with a little cytopathic effect on the L-02 cells, effectively reduce migration, adhesion and invasion ability of HCC cells. rpNK-lysin significantly reduce Fascin1 expression, which subsequently decrease β-catenin expression and metaloproteinases (MMP-2 and MMP9). This study suggest that MNTC rpNK-lysin has an anti-invasion and anti-metastasis effect on HCC cells in vitro through inhibition of Fascin 1 expression which regulates Wnt/β-catenin signaling pathway by inducing β-catenin degradation and subsequently results in suppression of MMP-2 and MMP9 expression.

CaP4: A 2.97 KDa Cationic Antibacterial Peptide from Curcuma pseudomontana L.

The present investigation reports the sequence of a 2.97KDa low molecular weight, cationic antibacterial peptide, caP4 isolated from wild variety of turmeric, Curcuma pseudomontana L. (Zingiberaceae). The rp-HPLC of 80% saturated ammonium sulphate protein precipitate showed four peaks labelled P1, P2, P3 and P4. The peak fraction, P4 eluted at 39.73 min showed 63.47% and 43.27% inhibition against E. coli and S. aureus respectively. The P4 was found to be stable at − 20 °C to 65 °C, in pH from 7.0 to 10.0 and retained antibacterial activity when treated with proteases. The MIC of P4 varied for different bacterial strains between 10 and 30 mg/L. Biofilm formation of P. aerugenosa and S. aureus was declined to 90% and 50% respectively at 20 µg of P4. The P4 on UPLC-MS yielded single major peak (with retention time of 1.98 min). The peak fraction was pooled and analysed using ESI-MS/MS, showing peptide masses ranging from 400 to 1800 Da. Further, Tof MS/MS-ESI of two intense peak yielded the sequences ASSCKPS (mass 1.16KDa) and ASSKWVAPSEW (mass 1.81 kDa) with a total mass of 2.97KDa, designated as caP4 (cationic peptide of Peak 4) having a net charge of +1 and hydrophobicity ranging from 18 to 22%. The above results show that caP4 could possibly be used as antibacterial peptide with significant therapeutic index.

Research Gate (RG) is a Meeting Point for Progress in Chemical Knowledge

Chemistry is one of the eldest and basic sciences. The technological progress is depending on progress in chemistry. Without evaluation of nature and preparation of a pure substance, it is not imaginable existence of modern biology, medicine, metallurgy and physics. All kind of existing technologies needs distinct in nature and pure in quality substances for existence and further progress. RG aims to bring together leading academic scientists, researchers and research scholars to exchange and share their experiences and research results on all aspects of chemistry and related fields. It also provides an interdisciplinary platform for researchers, practitioners and educators to present and discuss the most recent innovations, trends, and concerns as well as practical challenges encountered, and solutions adopted in the fields of chemistry. One of the nearly developed concepts in liquid chromatography is described in [1], which is a new type of liquid chromatography, the new technology as the Colloidal High-Performance Liquid Chromatography (CHPLC). This type of new technological approach in high-performance liquid chromatography is a simple time- and labor-saving one-step procedure suitable for analytical-, semipreparative-, and preparative-scale preparation of bacteriocins and other cationic antibacterial peptides as well as other cationic small molecular weight species. It allows to suspensions of bacterial cells, other colloidal and fast-particle materials, and dissolved anionic molecules passed through the column; however, cationic bacteriocins, small cationic peptides, organic cationic molecules and metal cations were separated by chromatography. The purity of the target substance generally at more than 95% was achieved by the judgment of spectral, chromatographic, and antimicrobial activity. In [1] was described the preparation, purification and chromatography of bacteriocin, bacitracin and lysozyme. It is my pleasure to invite all the great scientists, academicians, young researchers, students and everyone who is interested in Science, especially in chemistry from all over the world to attend the RG. All who are interested in theoretical and applicational aspects in Chemistry, New Materials Research and Nanotechnology will find them in RG. The topics as: Organic Chemistry and Advances in Organic Chemistry, Analytical Chemistry, Medicinal Chemistry, Clinical Chemistry, Forensic Chemistry, Industrial Chemistry and Occupational Chemistry, Food Chemistry, Green Chemistry and Chemical Renewable Resources, Agricultural and Food Chemistry, Physical and Theoretical Chemistry, Biological Chemistry, Marine Chemistry, Inorganic Chemistry, Environmental Chemistry, Nanoscience and Technology, Polymer Chemistry, Material Chemistry, Natural Resources Chemistry and Natural Products Chemistry, Electrochemistry, Geochemistry, Radio and Nuclear chemistry, Physical Chemistry, Theoretical Chemistry, Space (Interplanetary) Chemistry and many more are present on the pages of RG. At RG you will find the state-of-the-art research and cutting-edge theoretical and applicational technologies. The RG is covering a number of global aspects in Chemistry, New Materials Science and Nanotechnology from purely fundamental research up to practical applications.