Programmable enzymatic oxidation of tyrosine–lysine tetrapeptides

Abstract

Fmoc-capped tetrapeptides bearing two lysines and two tyrosines show programmable enzymatic activity. Solvent accessible tyrosines determine the extent of reactivity with tyrosinase, and subsequent quinone formation drives polymerisation.

Proton‐Conductive Melanin‐Like Fibers through Enzymatic Oxidation of a Self‐Assembling Peptide

“…Supramolecular self-assembly of short peptides is an attractive approach for construction of materials with structural and morphological properties that are defined across the molecular to the nano-and micrometer scale. [18][19][20] We have previously reported on the formation of melanin-like materials by using self-assembling tyrosine-tripeptides that pre-organize tyrosine side chains within supramolecular fibrous structures, which in turn serve as supramolecular substrates for enzymatic oxidative polymerization of tyrosine. Using a number of sequence isomers of peptides composed of tyrosine, phenylalanine, and aspartic acid, we could demonstrate that the peptide sequence dictates the self-assembly properties, and furthermore upon enzymatic oxidation provides access to a range of pigment materials with properties that are directly related to the selfassembly properties of the precursors.…”

Hollow Mesoporous Manganese Oxides: Application in Cancer Diagnosis and Therapy

“…A host of novel strategies for starvation therapy have been developed, including the competitive consumption of glucose and the block of the blood vessel. [ 113–115 ] The glucose can be effectively consumed by Gox to produce H 2 O 2 and gluconic acid in the presence of oxygen. HM‐MONs are generally applied in starvation therapy because the cascade reaction could accelerate glucose consumption; HM‐MONs could react with the glucose acid and H 2 O 2 to produce oxygen which is essential for efficient glucose depletion.…”

A novel tyrosine hyperoxidation enables selective peptide cleavage

“…48 Derived from this report one can posit that a mechanism for the DMP-mediated Ser-selective peptide rupture comprises (1) a C a -C b oxidative scission at the Ser site, yielding an acylimine, (2) water addition to the acylimine, which results in a carbinolamide moiety, (3) oxidation of the carbinolamide to an oxalamide and (4) hydrolytic cleavage of the oxalamide to generate peptide amide and oxalic acid mono amide as peptide N-and C-terminal fragments, respectively (Scheme S1 †). We then subjected the peptide Fmoc-Pro-Ser-Tyr-Pro-Ile-OH (21) to the DMPmediated cleavage reaction conditions. Aer two-days, equivalent amounts of the N-terminal fragments cleaved at both the Ser (20) and Tyr (22) sites were identied by HPLC (Fig.…”

“…The dopaquinone induced crosslinking of peptides and proteins usually proceeds via formation of Tyr-Tyr, 17 Tyr-Cys, 18 and Tyr-Lys 19 linkages and has been extensively applied in the development of moistureresistant adhesives and self-assembling materials for both industrial and biomedical applications. 20,21 Furthermore, the dopaquinone species can undergo Michael addition with secondary amines and anilines 22,23 or strain-promoted cycloaddition with cycloalkynes 24 to achieve selective protein conjugation. The oxidative cleavage of proteins at a Tyr site, however, has long been an underexplored area.…”