21. C-terminus Amidation Influences Biological Activity and Membrane Interaction of Maculatin 1.1
Cationic antimicrobial peptides have been investigated for their potential use in combating infections by targeting the cell membrane of microbes. Their unique chemical structure has been investigated to understand their mode of action and optimize their dose–response by rationale design. One common feature among cationic AMPs is an amidated C-terminus that provides greater stability against in vivo degradation.
20. Recent Applications of Aggregation Induced Emission Probes for Antimicrobial Peptide Studies
Antimicrobial peptides (AMPs) are being intensively investigated as they are considered promising alternatives to antibiotics where their clinical efficacy is dwindling due to the emergence of antimicrobial resistance (AMR). Accompanying with the development of AMPs, a number of fluorescent probes have been developed to facilitate the understanding the modes of action of AMPs.
![19. [Journal Cover] Chemically Modified and Conjugated Antimicrobial Peptides Against Superbugs](https://images.squarespace-cdn.com/content/v1/642d0cb753153160d6508469/1680840739806-W17GF5B1ZWXW8MG3PS13/3.5.jpg)
19. [Journal Cover] Chemically Modified and Conjugated Antimicrobial Peptides Against Superbugs
Antimicrobial resistance (AMR) is one of the greatest threats to human health that, by 2050, will lead to more deaths from bacterial infections than cancer. New antimicrobial agents, both broad-spectrum and selective, that do not induce AMR are urgently required. Antimicrobial peptides (AMPs) are a novel class of alternatives that possess potent activity against a wide range of Gram-negative and positive bacteria with little or no capacity to induce AMR.
18. Human Glucose-Dependent Insulinotropic Polypeptide (GIP) is an Antimicrobial Adjuvant Re-sensitising Multidrug-resistant Gram-negative Bacteria
ncreasing antibiotic resistance in Gram-negative bacteria has mandated the development of both novel antibiotics and alternative therapeutic strategies. Evidence of interplay between several gastrointestinal peptides and the gut microbiota led us to investigate potential and broad-spectrum roles for the incretin hormone, human glucose-dependent insulinotropic polypeptide (GIP) against the Enterobacteriaceae bacteria, Escherichia coli and Erwinia amylovora.
17. (Re)Defining the Proline-Rich Antimicrobial Peptide Family and the Identification of Putative New Members
As we rapidly approach a post-antibiotic era in which multi-drug resistant bacteria are ever-pervasive, antimicrobial peptides (AMPs) represent a promising class of compounds to help address this global issue. AMPs are best-known for their membrane-disruptive mode of action leading to bacteria cell lysis and death.
16. Chemical Modification of Cellulose Membranes for SPOT Synthesis
Since the development of solid-phase peptide synthesis in the 1960s, many laboratories have modified the technology for the production of peptide arrays to facilitate the discovery of novel peptide mimetics and therapeutics. One of these, known as SPOT synthesis, enables parallel peptide synthesis on cellulose paper sheets and has several advantages over other peptide arrays methods.
15. The 9-Fluorenylmethoxycarbonyl (Fmoc) Group in Chemical Peptide Synthesis – Its Past, Present, and Future
The chemical formation of the peptide bond has long fascinated and challenged organic chemists. It requires not only the activation of the carboxyl group of an amino acid but also the protection of the Nα-amino group.
14. Effect of Dimerized Melittin on Gastric Cancer Cells and Antibacterial Activity
Melittin is the peptide toxin found in bee venom and is effective against cancer cells. To enhance its activity, a branched dimeric form of melittin was designed. The monomeric form of the peptide was more cytotoxic against gastric cancer cells at low concentrations (1–5 μM) than the dimer form, while the cytotoxic effect was comparable at higher concentrations (10 μM).
13. Covalent Conjugation of Cationic Antimicrobial Peptides with a β-lactam Antibiotic Core
To combat the serious issue of increasing global antibiotic resistance, new antimicrobial therapies are urgently required. As one alternative, previously used antibiotics are being investigated for use in combination with more modern antibiotics including antimicrobial peptides.
12. The Effect of Selective D- or Nα-Methyl Arginine Substitution on the Activity of the Proline-Rich Antimicrobial Peptide, Chex1-Arg20
n vivo pharmacokinetics studies have shown that the proline-rich antimicrobial peptide, A3-APO, which is a discontinuous dimer of the peptide, Chex1-Arg20, undergoes degradation to small fragments at positions Pro6-Arg7 and Val19-Arg20. With the aim of minimizing or abolishing this degradation, a series of Chex1-Arg20 analogs were prepared via Fmoc/tBu solid phase peptide synthesis with D-arginine or, in some cases, peptide backbone Nα-methylated arginine, substitution at these sites.