We demonstrate a platform to screen a virus pseudotyped with Ebola virus glycoprotein (GP) against a library of peptides that contain non-natural amino acids to develop GP affinity ligands. This system could be used for rapid development of peptide-based antivirals for other emerging or neglected tropical infectious diseases.
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http://dx.doi.org/10.1039/c7cc08242h | DOI Listing |
Sheng Wu Gong Cheng Xue Bao
January 2025
College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou 310014, Zhejiang, China.
Transaminases are a class of enzymes that catalyze the transfer of amino between amino acids and keto acids, playing an important role in the biosynthesis of organic amines and the corresponding derivatives. However, natural enzymes often have low catalytic efficiency against non-natural substrates, which limits their widespread applications. Enzyme engineering serves as an effective approach to improve the catalytic properties and thereby expand the application scope of transaminases.
View Article and Find Full Text PDFChemistry
January 2025
Nano Medical Engineering Laboratory, RIKEN Cluster for Pioneering Research, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Protein immobilization technology is important in medical and industrial applications. We previously reported all-in-one in vitro selection, wherein a collagen-binding vascular endothelial growth factor (CB-VEGF) was identified from a fusion library of random and VEGF sequences. However, its interaction chemistry is mainly limited to the interaction established by the 20 canonical amino acids.
View Article and Find Full Text PDFJ Pept Sci
February 2025
Novo Nordisk Research Center Seattle, Novo Nordisk A/S, Seattle, Washington, USA.
We present PepFuNN, a new open-source version of the PepFun package with functions to study the chemical space of peptide libraries and perform structure-activity relationship analyses. PepFuNN is a Python package comprising five modules to study peptides with natural amino acids and, in some cases, sequences with non-natural amino acids based on the availability of a public monomer dictionary. The modules allow calculating physicochemical properties, performing similarity analysis using different peptide representations, clustering peptides using molecular fingerprints or calculated descriptors, designing peptide libraries based on specific requirements, and a module dedicated to extracting matched pairs from experimental campaigns to guide the selection of the most relevant mutations in design new rounds.
View Article and Find Full Text PDFToxins (Basel)
December 2024
Research Department for Limnology, University of Innsbruck, Mondseestrasse 9, 5310 Mondsee, Austria.
Recently, the use of click chemistry for localization of chemically modified cyanopeptides has been introduced, i.e., taking advantage of promiscuous adenylation (A) domains in non-ribosomal peptide synthesis (NRPS), allowing for the incorporation of clickable non-natural amino acids (non-AAs) into their peptide products.
View Article and Find Full Text PDFACS Synth Biol
January 2025
Institute of Agrobiological Sciences, National Agriculture and Food Research Organization (NARO), 1-2 Owashi, Tsukuba, Ibaraki 305-8634, Japan.
The domesticated silkworm , an essential industrial animal for silk production, has attracted attention as a host for protein production due to its remarkable protein synthesis capability. Here, we applied genetic code expansion (GCE) using a versatile pyrrolysyl-tRNA synthetase (PylRS)/tRNA pair from to ; GCE enables synthetic amino acid incorporation into proteins to give them non-natural functions. Transgenic lines expressing PylRS and its cognate tRNA were generated and cross-mated to obtain their F hybrid.
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