Vor kurzem hat die American Peptide Society eine Reihe von E-Seminaren durchgeführt. Der Vortrag von Jon Collins über optimierte Synthese- und Reinigungsstrategien für Peptide gibt neue Perspektiven in der Peptid-Synthese sowie in der Aufreinigung.
Ein weiterer Höhepunkt der Vortrag zur schnellen Produktion von Neoantigenen, synthetischen Proteinen und das Scale-up der mikrowellengestützten Peptidsynthese auf Hunderte von mmol. Dieses Seminar beinhaltete auch Vorträge von Prof. Dr. Fernando Albericio und einen Vortrag vom Doktoranden Chih-Te „Ted“ Zee.
#Peptidsynthese #Peptidaufreinigung #Prodigy #Liberty
Neues Jahr – Neuer Podcast!
Begleiten Sie Dr. Wendy Hartsock und andere Wissenschaftler in einer neuen Podcast-Serie über Peptide und Proteine. Die Gäste berichten von ihrer Forschung und Sie können von überall (sogar im Labor!) teilnehmen.
During the seminar we will discuss full scale flexibility of automative peptide synthesizers from CEM. We will present how to create peptide libraries for different screening projects: epitope mapping, receptor-ligand interactions, substitutional and lengh analysis. We will also present new peptide purification system, which will simplify and speed up the purification process of hydrophobic and long peptides, proteins. In the end we will learn how to use new green solvents for SPPS.
Peptid-Synthese mit umweltfreundlichem Lösemittel: Verwenden Sie TamiSolve in jedem SPPS-Prozess
– Niedrige Toxizität und Entflammbarkeit
– Hochwirksames Lösungsmittel für SPPS
– Hat keinen Einfluss auf die Lebensdauer von Aminosäurelösungen
– Erhältlich in großen Mengen
Giorgio Marini, Life Science Technical Specialist, will delve into this question in a free live webinar on 6th May, 14:00 – 15:00
Learn about how modern instrumentation revolutionizes peptide synthesis See how large scale cGMP peptide synthesis is achievable with microwave technology Document impurity profiles in days instead of weeks Discover how to offer next day custom and catalogue SPPS services
This is certainly one to sign up for.
Der Liberty PRIME Peptid-Synthesizer synthetisiert sehr effizient schwierige Konotoxine einschließlich einer neuartigen Sequenz (SxIIIC) von Conus striolatus, die eine einzigartige Eigenschaft zur Behandlung von neurologischen Erkrankungen hat.
Der Liberty PRIME™ Peptid-Synthesizer produziert Peptide außergewöhnlich schnell und mit hoher Effizienz und Reinheit. Erfahren Sie, wie mit Hilfe der CarboMAX-Kopplungsmethodik die Forschung zur Entwicklung von schnellen und spezifischen Antigen-basierten Assays für das SARS-CoV-2-Virus unterstützt wurde.
#Peptidsynthese #Corona #SARSCoV2
10. März 2021, ab 10.15 Uhr
Erleben Sie einen ganzen Tag interessante Vorträge zu den Neuigkeiten der Peptid-Synthese. Aufgrund der Corona-Situation können Präsenzvorträge derzeit nicht stattfinden. Deshalb veranstaltet CEM zusammen mit bekannten Forschern/innen dieses kostenfreie Online Seminar.
Academic Guest Speakers:
Professor Anna Maria Papini
University of Florence,
CY Cergy Paris Université
The challenge to design fully automated solid-phase MW-assisted cGMP ready processes of peptide production as active pharmaceutical ingredients
Interdepartmental Research Unit of Peptide & Protein Chemistry and Biology, Departments of Chemistry and NeuroFarBa, University of Florence (Italy)
With the increase of approved peptide-based drugs and patents expiring, the manufacturers’ need in production of peptides is dramatically rising. Companies involved in peptide-based drugs that have to be compliant with good manufacturing practices (GMP), face several challenges, such as high production costs on downstream processes (due to the use of high raw material amounts) and bad scalability. Therefore, the main challenge of production of active peptides as pharmaceutical ingredients is to find solutions to specific problems encountered during scale-up.
As a proof-of concept we will report the strategies we investigated for the preparation of Eptifibatide, scalable to kilogram-scale, having in common the use of the microwave-assisted solid-phase peptide synthesis (MW-SPPS) procedure, which is now available not only at R&D level but also for the large-scale manufacturing of peptides. Following the very fast microwave-assisted Fmoc/tBu synthesis of the Eptifibatide linear precursor by a DIC/Oxyma Pure coupling protocol at 90 °C, we explored both the solution (off-resin) and the solid-phase (on-resin) disulfide bond formation.
The relevance of the strategy we optimized is essentially based on the selection of the StBu orthogonal protection on cysteine that is easily removed by MPA acting as a novel reducing agent for Cys(StBu) deprotection. Moreover, we demonstrated that all operations can be performed by fully automated process in the instrumentation.
To the best of our knowledge, this is a unique strategy performing all the processes including disulfide bond formation in a single reactor and represents an optimized scalable fully automated solid-phase microwave-assisted cGMP-ready process to prepare Eptifibatide.
Designing Synthetic Peptides to Explore the Dark Matter of Protein Space
Schools of Chemistry and Biochemistry, & Bristol BioDesign Institute
University of Bristol, UK
Protein design—i.e., the construction of entirely new protein sequences that fold into prescribed structures—has come of age: it is now possible to generate a wide variety stable protein folds from scratch using rational and/or computational approaches. A new challenge for the field is to move past protein structures offered up by nature and to target the so-called ‘dark matter of protein space’; that is, protein structures that should be possible in terms of chemistry and physics, but which biology seems to have overlook or not used prolifically. This talk will illustrate what is currently possible in this nascent field using de novo a-helical coiled-coil peptides as building blocks for assembling larger, more-complex and functional protein-like structures.1
Coiled coils are bundles of 2 or more a helices that wrap around each other to form rope-like structures. They are one of the dominant structures that direct natural protein-protein interactions. Our understanding of coiled coils provides a strong basis for building new proteins from first principles. The first part of my talk will survey this understanding,1 our design methods,2,3 and our current “toolkit” of de novo coiled coils.4-5
Next, I will describe how the toolkit can be expanded used to generate some dark-matter protein structures. I’ll focus on the rational and computational design of a-helical barrel proteins, which have 5 or more helices surrounding accessible central channels.6 Finally, I’ll discuss how these synthetic barrel proteins can be put to use to make new nanotube materials,7 rudimentary catalysts,8 membrane-spanning pores,9 and the components of a new types of sensing devices.10
Professor Dek Woolfson
University of Bristol
Professor Fernando Albericio
University of Barcelona,
University of Kwazulu-Natal
Microwave-Assisted Solid-Phase Peptide Synthesis, A Unique Tool for Peptide Research
Fernando Albericio,1,2 Beatriz G. de la Torre1
1University of KwaZulu-Natal, Durban 4001, South Africa; 2University of Barcelona, 08028-Barcelona, Spain
During the last five years (2016-2020), 18 drugs containing peptides have been approved by the US FDA. In addition, several hundred are in clinical phases or advanced preclinical studies. The development of new synthetic strategies has facilitated this explosion in the world of peptides. In this regard, the development of new resins, coupling reagents, protecting groups, and, more importantly, reliable and robust peptide synthesizers have been vital for the consolidation of the peptide drug market.
In the field of automatic synthesizers, the last breakthrough occurred when at the beginning of this century, CEM launched the new concept of Microwave-Assisted SPPS. Our group and others have demonstrated that both couplings and Fmoc-removal are better performed in the microwave mode compared with classical synthesis or even with conventional heating. More important, this better performance in the two key reactions is not accompanied by any significant side-reaction.
This presentation will discuss our last results on the use of Microwave synthesis for the preparation of intriguing peptides and/or for developing new synthetic strategies: (i) the preparation of staple peptides via late-stage C(sp2)-H Pd activation using the microwave; (ii) synthesis of N-alkyl amino acid containing peptides; (iii) development of new and more efficient coupling reagents; and (iv) microwave-based Green Solid-Phase Peptide Synthesis (GSPPS).
In the GSPPS, the CEM Liberty Blue Microwave technology by itself could be considered green in terms of solvent consumption and time-saving and due to the excellent quality of the crude peptides, which enormously facilitates the purification with the consequent increase of yield and reduction of chromatography solvents.
Short antimicrobial peptides – discovery and optimization
Kai Hilpert, St George’s University
The global health threat surrounding bacterial resistance has resulted in antibiotic researchers shifting their focus away from ‘traditional’ antibiotics and concentrating on other antimicrobial agents, including antimicrobial peptides.
These peptides exhibit broad-spectrum activity against bacteria, including multi-drug resistant strains, viruses, fungi, and protozoa, and constitute a major element of the innate immune system of many multicellular organisms.
We use the Spot-synthesis technique to study and optimize naturally occurring as well as artificial antimicrobial peptides. Understanding the features that make them antibacterial and hemolytic allows for targeted drug development.
Associate Professor Kai Hilpert
St George’s University
Peptid-Synthese im Liberty Blue
The insulin-like peptide human relaxin-2 was identified as a hormone that, among other biological functions, mediates the hemodynamic changes occurring during pregnancy. Recombinant relaxin-2 (serelaxin) has shown beneficial effects in acute heart failure, but its full therapeutic potential has been hampered by its short half-life and the need for intravenous administration limiting its use to intensive care units. In this study, we report the development of long-acting potent single-chain relaxin peptide mimetics. Modifications in the B-chain of relaxin, such as the introduction of specific mutations and the trimming of the sequence to an optimal size, resulted in potent, structurally simplified peptide agonists of the relaxin receptor Relaxin Family Peptide Receptor 1 (RXFP1) (e.g., 54). Introduction of suitable spacers and fatty acids led to the identification of single-chain lipidated peptide agonists of RXFP1, with sub-nanomolar activity, high subcutaneous bioavailability, extended half-lives, and in vivo efficacy (e.g., 64).