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Best Paper Award 2022
Wiley and the European Peptide Society are pleased to announce the winner of the Journal of Peptide Science Best Paper Award in 2022. Many congratulations to the authors for their award-winning article.
Effects of N‐terminal modifications on the stability of antimicrobial peptide SAMP‐A4 analogues against protease degradation
Graphical Abstract
N-terminal fatty acid coupling increased the antimicrobial activities and biostabilities of SAMP-A4 analogues in trypsin solutions and plasma, and the activities and stabilities improved with increasing fatty acid chain length.
Articles
Breaking down and building up alpha‐synuclein: An insight on its N‐terminal domain
- 30 November 2023
Graphical Abstract
A library of peptides, deriving from both native and Parkinson's disease (PD) mutated sequences of the N-terminal domain of alpha-synuclein (αSyn), was synthesized. Their secondary structure was characterized in order to evaluate the effect of PD mutations. The kinetics of polymerizing tubulin in vitro in the presence of the peptides was evaluated.
Antiviral peptides inhibiting the main protease of SARS‐CoV‐2 investigated by computational screening and in vitro protease assay
- 29 November 2023
Graphical Abstract
The therapeutic value of 67 peptides targeting the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease (Mpro) was investigated using molecular docking. Molecular dynamics simulations on eight protein–peptide complexes revealed that temporin L, indolicidin, and lymphocytic choriomeningitis virus (LCMV) GP1 are the best candidates in terms of stability, interaction, and structural compactness.
Cysteine‐free cone snail venom peptides: Classification of precursor proteins and identification of mature peptides
- 27 November 2023
Graphical Abstract
Twenty acyclic peptides from Conus monile and Conus betulinus were identified, with the common modifications of C-terminus amidation, gamma carboxylation of glutamic acid, N-terminus conversion of Gln to a pyroglutamyl residue, and hydroxylation of Pro to Hyp. Proteolytic trimming of sequences by cleavage at the C-terminus of Asn residues is established.
Exploring biocompatible chemistry to create stapled and photoswitchable variants of the antimicrobial peptide aurein 1.2
- 5 November 2023
Graphical Abstract
Stapled α-helical versions of aurein 1.2 were developed using biocompatible conjugation chemistry between dicyanopyridine and 1,2-aminothiols. A double-cysteine variant stapled with perfluoro azobenzene at i, i + 7 exhibited a change in overall helicity induced by light. The applicability of this staple to attach to cysteine residues in i, i + 7 positions of a helix in a model protein is demonstrated.
The following is a list of the most cited articles based on citations published in the last three years, according to CrossRef.
Advances in Fmoc solid‐phase peptide synthesis
- 4-27
- 20 January 2016
Graphical Abstract
Almost 40 years after its introduction, Fmoc/tert-butyl chemistry is still an area of dynamic research. This review examines the latest advances in the method and highlights scope for further developments.
Self-assembling amphiphilic peptides
- 453-467
- 13 April 2014
Graphical Abstract
The self-assembly of amphiphilic peptides including surfactant-like peptides and lipopeptides is reviewed, focusing on modes and mechanisms of self-assembly as well as applications in biomedicine and materials science.
Relationship of sidechain hydrophobicity and α‐helical propensity on the stability of the single‐stranded amphipathic α‐helix
- 319-329
- September/October 1995
Bacterial membrane lipids in the action of antimicrobial agents
- 298-305
- 30 November 2010
Graphical Abstract
A mechanism contributing to the antimicrobial action of certain agents is illustrated. The effect is a consequence of rearrangements of the bacterial membrane as a consequence of the interaction of a polycationic peptide (blue) selectively interacting with anionic lipid components (red) in the membrane and causing these lipids to cluster in a separate region of the membrane.
Cell penetration: scope and limitations by the application of cell‐penetrating peptides
- 760-784
- 11 August 2014
Graphical Abstract
Penetration of polar or badly soluble compounds through the membrane of live cells requires support. Cell-penetrating peptides (CPPs) are very promising chemical helpers, particularly favored for clinical applications. This review describes a wide array of differing CPPs, cargos, and cell lines. The application of CPPs is compared with other physical or chemical methods. Promising developments such as enhancement of cell specificity, specific transport into cell organelles, and the transport of drugs into tissues and organs are discussed together with the overall scope and limitations.
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