Recent Peptide Research and News
Reflecting work in the van der Donk Group
Ribosomally synthesized and posttranslationally modified peptides, RiPPs, represent one of the most structurally diverse classes of natural products, yet many RiPP families remain biosynthetically uncharacterized...
Reflecting work in the The Tal-Gan Group
Streptococcus constellatus, a member of the Streptococcus anginosus group, SAG, is an opportunistic pathogen commonly found in the human oral and gastrointestinal microbiota. While often commensal, it has increasingly been implicated in severe purulent infections, particularly in immunocompromised individuals. Despite its emerging clinical relevance...
Reflecting work in the Proulx Group
This study demonstrates that a key determinant of this reactivity is the choice of solvent. By shifting from aqueous buffer to a mixed organic solvent system, MeOH/DCE, the authors observed a pronounced shift in the oxidation pathway, favoring productive...
Reflecting work in the The Süssmuth Group
In this study, researchers from the Süssmuth group at the Technische Universität Berlin, published in the Journal of the American Chemical Society, elucidated the structure of AFC-BC11 as an N-acyl tetrapeptide with a distinctive architecture. The molecule is...
Reflecting work in the Dahlén and Andaloussi Groups
In this collaborative study, published in Bioconjugate Chemistry by researchers from the Dahlén group at Astra-Zeneca, Gothenburg, Sweden, and the Andaloussi team at the Karolinska Institutet, Stockholm, Sweden, the authors present...
Reflecting work in the Wilson Lab
Protein–protein interactions, PPIs, are fundamental to cellular regulation, yet targeting them therapeutically remains challenging due to their extensive, shallow interfaces. Peptides offer an attractive solution, providing structural fidelity...
Reflecting work in the Kwon Lab
Traumatic brain injury, TBI, remains a profound and unresolved clinical challenge, responsible for long-term disability in both civilian and military populations. The lack of effective pharmacological interventions...
Reflecting work in the Tal-Gan Lab
Streptococcus cristatus, a commensal member of the oral microbiota and recently reclassified from Streptococcus oligofermentans, has emerged as a promising candidate in the pursuit of biotherapeutics targeting oral pathogens. A comprehensive...
Reflecting work in the Carik and Malins Labs
This comprehensive review from the labs of David Craik and Lara Malins at Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, at the University of Queensland, published in Biochemistry, highlights the powerful...
Reflecting work in the Schneider Lab
Published in the Journal of the American Chemical Society, researchers in the lab of Dr. Joel P. Schneider at NIH, have unveiled a groundbreaking molecular design strategy that shifts gel-forming peptides into the crystalline state...
Reflecting work in the Arora Group
In a major step forward, researchers in the Arora Group at the New York University, have now developed a rationally designed proteomimetic receptor capable of selectively trapping MYC in its biologically active conformation...
Reflecting work in the Liu Lab
Published as an ASAP article in the Journal of the American Chemical Society, researchers from the Wenshe Liu Lab at Texas A&M, currenly our "Lab of the Month," present the development...
Reflecting work in the Mitchell Lab
Cyclopropane-containing amino acids, prized for their conformational rigidity and stability, are of increasing interest in therapeutic peptide development and antimicrobial drug discovery. A recent study from Nicholas Mitchell’s group at the University of Nottingham...
Reflecting work in the Woolfson Lab
The Woolfson Lab continues to break new ground in de novo protein design with the successful creation of mixed-charge A3B3 heterohexameric α-helical barrels, αHBs, assembled from distinct acidic, A, and basic, B, peptide chains. Drawing on...
Reflecting work in the Niitsu Lab
Membrane-spanning peptides that form ion-conductive channels remain a challenging frontier in de novo protein design. While strides have been made in creating water-soluble peptide assemblies, translating that precision to transmembrane systems...
Reflecting work in the D'Amelio Lab
As antibiotic resistance surges worldwide, the search for effective new therapeutics has led scientists to a surprising source: the venom of Bungarus fasciatus, the banded krait. From this venom, researchers have isolated Cathelicidin-BF...
Reflecting work in the Tezcan Group
Isopeptide bonds, IPBs, — covalent linkages between the side chains of lysine and asparagine/glutamine or aspartate/glutamate — are remarkable for their chemical resilience and structural significance...
Reflecting work in the Raj Lab
The selective incorporation of post-translational modifications, PTMs, into proteins remains a key challenge in chemical biology, particularly for modifications like arginine carbonylation, which plays a crucial role...
Automated Peptide Synthesis
In this sponsored content by Gyros Protein Technologies, discover how automated systems revolutionize peptide production with enhanced efficiency and reproducibility.
The evolution from manual to automated solid-phase peptide synthesis, SPPS, has transformed research workflows, significantly reducing human error while enabling walk-away operations and parallel processing capabilities.
Advanced features like microfluidic design, induction heating, and real-time UV monitoring create optimal conditions even for challenging sequences, substantially improving yield and purity. This article shows you how to harness these innovations for your peptide research needs.
The Nicola D'Amelio Lab
The D’Amelio Lab is part of the Enzyme and Cell Engineering Unit, UMR 7025 CNRS, with active sites at Université de Picardie Jules Verne, UPJV, in Amiens and Université de Technologie de Compiègne, UTC, in Compiègne, France. Co-directed by Professors Karsten Haupt, Bérangère Avalle, and Catherine Sarazin, the lab is led by Professor Nicola D’Amelio and is internationally recognized for its work in structural biology, biomedicine, and peptide engineering.
Professor D’Amelio’s team is at the forefront of peptide-based research targeting antimicrobial resistance, cancer, and neurodegenerative disease. Their ADAPTABLE platform—an interactive database of antimicrobial peptides—guides the rational design of therapeutic peptides, while ongoing projects explore peptide interference in cancer signaling, microbiome-based delivery systems, and blood-brain barrier-penetrating therapeutics for Alzheimer’s.
Stay tuned for more lab features, and don’t miss the chance to get your lab featured!
Please contact Lars Sahl to get involved!
What Current Members Say
“I have been a member of APS since I was a graduate student because of the benefits and opportunities it provided scientists at that stage of my career. Through the years, I have continued to be a member so I can engage with the top researchers working in peptide science from around the globe.”
Marcos Pires
Associate Professor of Chemistry
University of Virginia
“APS provides a forum for connecting graduate students, postdocs and working professionals with each other based on shared professional skills and interests. When it comes time to look for their next position, APS members can count on a strong network of like-minded scientists who value their skills and accomplishments.”
Joshua Kritzer
Professor
Tufts University
“Being a member of the American Peptide Society and attending the Peptide Symposium, one of the key asset of the society, I have gain new perspectives on emerging peptide technologies, and gain insights about current challenges from prominent peptide leaders. It is a great society for the education and professional development for our peptide scientist.”
Ved Srivastava
Ph.D., Vice President of Peptide Chemistry
Intarcia Therapeutics
Peptide Synthesis for Beginners
Explore this in-depth tutorial on peptide synthesis, featuring contributions from the APS Website Committee and other researchers in the field.
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