Biomaterial Database

Of Thiols and Disulfides: Methods for Chemoselective Formation of Asymmetric Disulfides in Synthetic Peptides and Polymers. 2018

Olga Schäfer, and Matthias Barz

Institute of Organic Chemistry, Johannes Gutenberg University Mainz, Duesbergweg 10-14, 55128, Mainz, Germany.

In protein or peptide chemistry, thiols are frequently chosen as a chemical entity for chemoselective modification reactions. Although it is a well-established methodology to address cysteines and homocysteines in aqueous media to form S-C bonds, possibilities for the chemoselective formation of asymmetric disulfides have been less approached. Focusing on bioreversibility in conjugation chemistry, the formation of disulfide bonds is highly desirable for the attachment of thiol-containing bioactive agents to proteins or in cross-linking reactions, because disulfide bonds can combine stability in blood with degradability inside cells. In this Concept article, recent approaches in the field of activating groups for thiol moieties incorporated in peptide and polymer materials are highlighted. Advantageous combinations of stability during synthesis of the material with high reactivity towards thiols are explored focusing on simplification and prevention of side reactions as well as additional deprotection and activation steps prior to disulfide formation. Moreover, applications of this chemistry are highlighted and future perspectives are envisioned.

UI	MeSH Term	Description	Entries
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D011108	Polymers	Compounds formed by the joining of smaller, usually repeating, units linked by covalent bonds. These compounds often form large macromolecules (e.g., BIOPOLYMERS; PLASTICS).	Polymer
D011789	Quantum Theory	The theory that the radiation and absorption of energy take place in definite quantities called quanta (E) which vary in size and are defined by the equation E	Quantum Theories,Theories, Quantum,Theory, Quantum
D004220	Disulfides	Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.	Disulfide
D005609	Free Radicals	Highly reactive molecules with an unsatisfied electron valence pair. Free radicals are produced in both normal and pathological processes. Free radicals include reactive oxygen and nitrogen species (RONS). They are proven or suspected agents of tissue damage in a wide variety of circumstances including radiation, damage from environment chemicals, and aging. Natural and pharmacological prevention of free radical damage is being actively investigated.	Free Radical
D013438	Sulfhydryl Compounds	Compounds containing the -SH radical.	Mercaptan,Mercapto Compounds,Sulfhydryl Compound,Thiol,Thiols,Mercaptans,Compound, Sulfhydryl,Compounds, Mercapto,Compounds, Sulfhydryl
D058105	Polymerization	Chemical reaction in which monomeric components are combined to form POLYMERS (e.g., POLYMETHYLMETHACRYLATE).	Polymerizations
D060327	Solid-Phase Synthesis Techniques	Techniques used to synthesize chemicals using molecular substrates that are bound to a solid surface. Typically a series of reactions are conducted on the bound substrate that results in either the covalent attachment of specific moieties or the modification of existing function groups. These techniques offer an advantage to those involving solution reactions in that the substrate compound does not have to be isolated and purified between the reaction steps.	Solid-Phase Synthesis,Peptide Synthesis, Solid-Phase,Solid-Phase Nucleotide Synthesis,Solid-Phase Nucleotide Synthesis Techniques,Solid-Phase Peptide Synthesis,Solid-Phase Peptide Synthesis Techniques,Solid-Phase Synthesis Methods,Synthesis, Solid-Phase,Method, Solid-Phase Synthesis,Methods, Solid-Phase Synthesis,Nucleotide Syntheses, Solid-Phase,Nucleotide Synthesis, Solid-Phase,Peptide Syntheses, Solid-Phase,Peptide Synthesis, Solid Phase,Solid Phase Nucleotide Synthesis,Solid Phase Nucleotide Synthesis Techniques,Solid Phase Peptide Synthesis,Solid Phase Peptide Synthesis Techniques,Solid Phase Synthesis,Solid Phase Synthesis Methods,Solid Phase Synthesis Techniques,Solid-Phase Nucleotide Syntheses,Solid-Phase Peptide Syntheses,Solid-Phase Syntheses,Solid-Phase Synthesis Method,Solid-Phase Synthesis Technique,Syntheses, Solid-Phase,Syntheses, Solid-Phase Nucleotide,Syntheses, Solid-Phase Peptide,Synthesis Method, Solid-Phase,Synthesis Methods, Solid-Phase,Synthesis Technique, Solid-Phase,Synthesis Techniques, Solid-Phase,Synthesis, Solid Phase,Synthesis, Solid-Phase Nucleotide,Synthesis, Solid-Phase Peptide,Technique, Solid-Phase Synthesis,Techniques, Solid-Phase Synthesis
D018625	Microscopy, Atomic Force	A type of scanning probe microscopy in which a probe systematically rides across the surface of a sample being scanned in a raster pattern. The vertical position is recorded as a spring attached to the probe rises and falls in response to peaks and valleys on the surface. These deflections produce a topographic map of the sample.	Atomic Force Microscopy,Force Microscopy,Scanning Force Microscopy,Atomic Force Microscopies,Force Microscopies,Force Microscopies, Scanning,Force Microscopy, Scanning,Microscopies, Atomic Force,Microscopies, Force,Microscopies, Scanning Force,Microscopy, Force,Microscopy, Scanning Force,Scanning Force Microscopies