https://journal.riverpublishers.com/index.php/jsame/issue/feed 2026-01-01T03:29:53+00:00 Editorial Office Manager jsame@riverpublishers.com Open Journal Systems <div class="JL3"> <div class="journalboxline"> <p><strong>Aims:</strong></p> <p>Self-Assembly and Molecular Electronics (SAME) is a multidisciplinary <strong>peer-reviewed open access</strong> journal covering the areas of molecular electronics, self assembly and Nanotechnology, with the aim to develop novel bottom - up approaches for the design and manufacturing of functional devices. SAME encourages original cross-disciplinary full research articles, rapid communications of important new scientific and technological findings and state-of-the-art reviews.<br /><br /><strong>Scope:</strong><br /><br />SAME publishes theoretical and experimental <strong>original research</strong> and review articles, covering the areas of:<br /><br /></p> <ul class="botL"> <li class="show">Molecular Electronics and Molecular Devices with a particular emphasis on DNA, peptide and protein based systems</li> <li class="show">Self Assembly in Nanosience, Chemistry, Biology, synthetic Biology and Medicine</li> <li class="show">Supramolecular Chemistry</li> <li class="show">Modelling of Structural and Electronical Properties of Organic Molecules and Self Assembled Systems</li> <li class="show">Atomic Force Microscopy and other scanning probe techniques</li> <li class="show">Spectroscopic studies of nanostructures on surfaces and in solution including femtosecond and terahertz spectroscopy studies</li> <li class="show">Studies of electron transfer including electrochemical approaches</li> <li class="show">Applications of nanostructures in bio-sensing and plasmonics</li> </ul> <br /> <p>SAME also features a <strong>Method Section</strong>, devoted to in-depth description of the novel and standard methods in the field. Contributions to this section follow the usual journal submission guidelines and formats. Additionally, video tutorials and computer code are particularly encouraged to be included as supplements to the submissions to this section.</p> <p> </p> <br /><br /> <p>This is an <strong>Open Access</strong> journal, and conform our Open Access policy authors will be charged an Article Processing Charge of EUR 500 after their article is submitted and reviewed, and if it is accepted. All Open Access articles are published and distributed under the Creative Commons Attribution-Non Commercial 4.0 International (CC BY-NC 4.0). <br /><br />Authors may apply for a waiver on the Article Processing Charge, for this please contact <a href="mailto:info@riverpublishers.com">info@riverpublishers.com</a></p> </div> </div> <p> </p> https://journal.riverpublishers.com/index.php/jsame/article/view/478 2026-01-01T03:18:02+00:00 Julia Petersen julia.petersen18@gmx.com Katrine G. Eskildsen katrine@eskild.cn Peter Fojan fp@mp.aau.com

<p>Self-assembled peptides have been a research focus for the last 50 years. At the same time, metallic nanoparticles have become a subject of interest, especially in the areas of photonics and surface plasmon enhancement. The properties of these two systems, combined with fluorescence, yield a very sensitive bio-assay. To achieve the biosensor, a De Novo peptide has been designed. This novel α-helix design contains a recognition motif for a TEV-protease as a model sensor. The prediction of the peptide structure is based on AI-based methods. AlphaFold [1] and PEP-FOLD [2] implementations of the AI algorithms have been used for the analysis. Experimental verification of the peptide properties have been achieved by solid phase peptide synthesis (SPPS) and followed by biophysical methods such as circular dichroism (CD) to verify the secondary structure, atomic force microscopy (AFM) to investigate the self-assembling properties of the gold nanoparticles (AuNPs) and surface plasmon resonance spectroscopy (SPR) for real-time binding and release studies. The experimental data are supplemented with molecular dynamics (MD) simulations. The self-assembly behaviour seen in the MD simulation agrees well with the images obtained by AFM. Simulation of peptide denaturation yields a denaturation temperature above 57^∘C.</p>

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