Author: Gonzalez-Castro, Rafael; Gomez-Lim, Miguel Angel; Plisson, Fabien
Title: Cysteine-rich peptides: hyperstable scaffolds for protein engineering. Cord-id: 4yuonqmt Document date: 2020_10_23
ID: 4yuonqmt
Snippet: Cysteine-rich peptides (CRPs) are small proteins of less than 100 amino acids in length characterized by the presence of disulfide bridges and common end-to-end macrocyclization. These properties confer hyperstability against high temperatures, salt concentration, serum presence, and protease degradation to CRPs. Besides, their inter-cysteine domains (loops) are susceptible to residue hypervariability. CRPs have been successfully applied as stable scaffolds for molecular grafting, a protein engi
Document: Cysteine-rich peptides (CRPs) are small proteins of less than 100 amino acids in length characterized by the presence of disulfide bridges and common end-to-end macrocyclization. These properties confer hyperstability against high temperatures, salt concentration, serum presence, and protease degradation to CRPs. Besides, their inter-cysteine domains (loops) are susceptible to residue hypervariability. CRPs have been successfully applied as stable scaffolds for molecular grafting, a protein engineering process where cysteine-rich structures provide higher thermodynamic and metabolic stability to an epitope and acquire new biological function(s). This review describes successes and limitations for six cysteine-rich scaffolds, their bioactive epitopes, and the resulting grafted peptides.
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