Publication

PSEUDO-PROLINES (PSI-PRO) FOR ACCESSING INACCESSIBLE PEPTIDES

1995
Journal Articles

Abstract

Pseudo-prolines (Psi Pro) are introduced as a temporary protection technique for serine, threonine and cysteine side chains in standard Fmoc/tBu solid-phase peptide synthesis (SPPS). The incorporation of these novel building blocks into a growing peptide chain proceeds by means of the coupling of preformed, suitably protected Psi Pro dipeptides. For the example of representative model peptides used in protein de novo design, the potential of Psi Pro, to solubilize otherwise sparingly or completely insoluble peptides is demonstrated. Because of their intrinsic propensity for preventing peptide aggregation and beta-sheet formation, pseudo-prolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques.

Official source

https://infoscience.epfl.ch/entities/publication/8f487a83-9418-4176-ac4c-8eff28db5a25

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1995
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/8f487a83-9418-4176-ac4c-8eff28db5a25

About this result

Related concepts (24)

Peptide synthesis

In organic chemistry, peptide synthesis is the production of peptides, compounds where multiple amino acids are linked via amide bonds, also known as peptide bonds. Peptides are chemically synthesized by the condensation reaction of the carboxyl group of one amino acid to the amino group of another. Protecting group strategies are usually necessary to prevent undesirable side reactions with the various amino acid side chains. Chemical peptide synthesis most commonly starts at the carboxyl end of the peptide (C-terminus), and proceeds toward the amino-terminus (N-terminus).

Intrinsically disordered proteins

In molecular biology, an intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure, typically in the absence of its macromolecular interaction partners, such as other proteins or RNA. IDPs range from fully unstructured to partially structured and include random coil, molten globule-like aggregates, or flexible linkers in large multi-domain proteins. They are sometimes considered as a separate class of proteins along with globular, fibrous and membrane proteins.

Beta sheet

The beta sheet, (β-sheet) (also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The supramolecular association of β-sheets has been implicated in the formation of the fibrils and protein aggregates observed in amyloidosis, Alzheimer's disease and other proteinopathies.

Related publications (11)

PSEUDO-PROLINES (PSI-PRO) FOR ACCESSING INACCESSIBLE PEPTIDES

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Single-Molecule Fingerprinting of Unlabeled Full-Length Proteins Using an Aerolysin Nanopore

Strategic Template Filtering Accelerates Fragment-Based Peptide Docking

Of Revolutions and Roadblocks: The Emerging Role of Machine Learning in Biocatalysis