Amino acids, Peptidomimetics, peptides, protein InteractionS group
The design and synthesis of a series of peptide derivatives based on a short ACE2 α-helix 1 epitope and subsequent [i – i+4] stapling of the secondary structure resulted in the identification of a...
Lysozyme (E.C. 3.2.1.17), an about 14 kDa protein and pI 11, widely spread in nature, is present in humans mainly in milk, saliva, and intestinal mucus as a part of innate defense mechanisms.It is...
Protein-mimetic peptides (PMPs) are shorter sequences of self-assembling proteins, that represent remarkable building blocks for the generation of bioinspired functional supramolecular structures with multiple applications.The identification of novel aminoacidic sequences that permit the access...
Alpha-synuclein (αSyn) is a small presynaptic protein (14 kDa) that is involved in synucleinopathies including Parkinson’s disease (PD). In its native state, the αSyn monomer exists in an unfolded state, and its folding is...
Protein aggregation into amyloid fibrils is the archetype of aberrant biomolecular selfassembly processes, with more than 50 associated diseases that are mostly uncurable.Understanding aggregation mechanisms is thus of fundamental importance and goes inparallel with...
Gelsolin amyloidosis (AGel) is characterized by multiple systemic and ophthalmic features resulting from pathological tissue deposition of the gelsolin (GSN) protein. To date, no cure is available for the treatment of any form of...
Although a plethora of chemistries have been developed to selectively decorate protein molecules, novel strategies continue to be reported with the final aim of improving selectivity and mildness of the reaction conditions, preserve protein...
application / proteins / unnatural amino acid
di emanuela erba · Published 6 Aprile 2022 · Last modified 13 Maggio 2022
Alpha-synuclein (αSyn) is a highly expressed and conserved protein, typically found in the presynaptic terminals of neurons. Themisfolding and aggregation of αSyn into amyloid fibrils is a pathogenic hallmark of several neurodegenerative diseases called...
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