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Breaking a Couple: Disulfide Reducing Agents
Authors:Sinenhlanhla N Mthembu  Dr Anamika Sharma  Prof Fernando Albericio  Prof Beatriz G de la Torre
Affiliation:1. Peptide Science Laboratory, School of Chemistry and Physics, University of KwaZulu-Natal, Durban, 4001 South Africa

KRISP, School of Laboratory of Medicine and Medical Sciences College of Health Sciences, University of KwaZulu-Natal Westville, Durban, 4001 South Africa;2. Peptide Science Laboratory, School of Chemistry and Physics, University of KwaZulu-Natal, Durban, 4001 South Africa;3. KRISP, School of Laboratory of Medicine and Medical Sciences College of Health Sciences, University of KwaZulu-Natal Westville, Durban, 4001 South Africa

Abstract:Cysteine is present in a large number of natural and synthetic (bio)molecules. Although the thiol side chain of Cys can be in a free form, in most cases it forms a disulfide bond either with a second Cys (bridge) or with another thiol, as in the case of protecting groups. Efficient reduction of these disulfide bridges is a requirement for many applications of Cys-containing molecules in the fields of chemistry and biochemistry. Here we review reducing methods for disulfide bonds, taking into consideration the solubility of the substrates when selecting the appropriate reducing reagent.
Keywords:Cysteine  cystine  disulfide bridges  reducing agents  solid-phase peptide synthesis
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